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- PDB-6fec: Human cap-dependent 48S pre-initiation complex -

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Basic information

Entry
Database: PDB / ID: 6fec
TitleHuman cap-dependent 48S pre-initiation complex
Components
  • (40S ribosomal protein ...) x 31
  • (EUKARYOTIC TRANSLATION INITIATION FACTOR ...) x 14
  • 18S ribosomal RNA
  • Messenger RNA (26-MER)
  • Receptor of activated protein C kinase 1
  • Transfer RNA (75-MER)
  • Ubiquitin-40S ribosomal protein S27a
KeywordsRIBOSOME / Translation initiation / 48S complex / capped mRNA / initiation factor 4B / start codon recognition
Function / homology
Function and homology information


eukaryotic translation initiation factor 4F complex assembly / RNA strand-exchange activity / viral translational termination-reinitiation / eukaryotic translation initiation factor 3 complex, eIF3e / positive regulation of mRNA binding / eukaryotic translation initiation factor 3 complex, eIF3m / eukaryotic translation initiation factor 2 complex / RNA strand annealing activity / translation factor activity, RNA binding / eukaryotic translation initiation factor 3 complex ...eukaryotic translation initiation factor 4F complex assembly / RNA strand-exchange activity / viral translational termination-reinitiation / eukaryotic translation initiation factor 3 complex, eIF3e / positive regulation of mRNA binding / eukaryotic translation initiation factor 3 complex, eIF3m / eukaryotic translation initiation factor 2 complex / RNA strand annealing activity / translation factor activity, RNA binding / eukaryotic translation initiation factor 3 complex / cytoplasmic translational initiation / eukaryotic 43S preinitiation complex / eukaryotic translation initiation factor 4F complex / protein tyrosine kinase inhibitor activity / positive regulation of gastrulation / protein-synthesizing GTPase / positive regulation of Golgi to plasma membrane protein transport / negative regulation of RNA splicing / IRE1-RACK1-PP2A complex / eukaryotic 48S preinitiation complex / formation of translation preinitiation complex / ubiquitin ligase inhibitor activity / formation of cytoplasmic translation initiation complex / laminin receptor activity / cytoplasmic side of rough endoplasmic reticulum membrane / regulation of cell division / negative regulation of endoplasmic reticulum unfolded protein response / negative regulation of hydrogen peroxide-induced neuron death / positive regulation of base-excision repair / negative regulation of DNA repair / positive regulation of DNA N-glycosylase activity / response to TNF agonist / oxidized pyrimidine DNA binding / negative regulation of ubiquitin protein ligase activity / positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage / positive regulation of cysteine-type endopeptidase activity involved in execution phase of apoptosis / positive regulation of ceramide biosynthetic process / erythrocyte homeostasis / regulation of translational initiation / mammalian oogenesis stage / NF-kappaB complex / negative regulation of phagocytosis / regulation of establishment of cell polarity / positive regulation of endodeoxyribonuclease activity / signaling adaptor activity / negative regulation of Wnt signaling pathway / cysteine-type endopeptidase activator activity involved in apoptotic process / oxidized purine DNA binding / protein targeting to peroxisome / activation-induced cell death of T cells / protein kinase A binding / supercoiled DNA binding / positive regulation of mitochondrial depolarization / translation regulator activity / phagocytic cup / ion channel inhibitor activity / negative regulation of smoothened signaling pathway / positive regulation of apoptotic signaling pathway / ubiquitin-like protein conjugating enzyme binding / iron-sulfur cluster binding / positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator / rescue of stalled ribosome / positive regulation of T cell receptor signaling pathway / poly(U) RNA binding / stress granule assembly / DNA-(apurinic or apyrimidinic site) lyase / class I DNA-(apurinic or apyrimidinic site) endonuclease activity / BH3 domain binding / DNA-(apurinic or apyrimidinic site) endonuclease activity / positive regulation of activated T cell proliferation / erythrocyte development / GABA-ergic synapse / positive regulation of cyclic-nucleotide phosphodiesterase activity / TOR signaling / ribosomal small subunit export from nucleus / ribosomal small subunit binding / regulation of tumor necrosis factor-mediated signaling pathway / maturation of SSU-rRNA / regulation of translational fidelity / negative regulation of protein kinase B signaling / T cell proliferation involved in immune response / spindle assembly / negative regulation of ubiquitin-dependent protein catabolic process / small-subunit processome / positive regulation of JUN kinase activity / SRP-dependent cotranslational protein targeting to membrane / ribosomal small subunit biogenesis / gastrulation / translation initiation factor binding / positive regulation of DNA repair / molecular adaptor activity / negative regulation of translational initiation / positive regulation of microtubule polymerization / polysome / nuclear-transcribed mRNA catabolic process, nonsense-mediated decay / laminin binding / positive regulation of cell cycle / negative regulation of peptidyl-serine phosphorylation / Hsp70 protein binding / translation initiation factor activity
RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain) / Nucleic acid-binding, OB-fold / Ribosomal protein S5 domain 2-type fold, subgroup / Ribosomal protein S6, eukaryotic / Ribosomal protein S4e, central region / Ribosomal protein S4e, N-terminal / Ribosomal protein L23/L15e core domain superfamily / Nucleotide-binding alpha-beta plait domain superfamily / Ribosomal protein S13/S15, N-terminal / Tetratricopeptide-like helical domain superfamily ...RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain) / Nucleic acid-binding, OB-fold / Ribosomal protein S5 domain 2-type fold, subgroup / Ribosomal protein S6, eukaryotic / Ribosomal protein S4e, central region / Ribosomal protein S4e, N-terminal / Ribosomal protein L23/L15e core domain superfamily / Nucleotide-binding alpha-beta plait domain superfamily / Ribosomal protein S13/S15, N-terminal / Tetratricopeptide-like helical domain superfamily / Initiation factor eIF2 gamma, C-terminal / Zinc-binding ribosomal protein / Ribosomal protein S13-like, H2TH / Eukaryotic translation initiation factor 3 subunit K / S15/NS1, RNA-binding / K homology domain superfamily, prokaryotic type / Translation elongation factor EF1A/initiation factor IF2gamma, C-terminal / Translation protein, beta-barrel domain superfamily / Ribosomal protein S30 / Ribosomal protein L2, domain 2 / WD40/YVTN repeat-like-containing domain superfamily / KOW / Ribosomal protein S10, conserved site / Translation initiation factor 3 complex subunit L / Eukaryotic translation initiation factor 3 subunit E, N-terminal / Ribosomal protein S6e, conserved site / Ribosomal protein S3Ae, conserved site / Ribosomal protein S3, conserved site / Ribosomal protein S17e, conserved site / Ribosomal protein S14, conserved site / Ribosomal protein S13, conserved site / Ribosomal protein S4e, N-terminal, conserved site / K homology domain-like, alpha/beta / Ribosomal protein S2, conserved site / Ribosomal S11, conserved site / Ribosomal S24e conserved site / Ribosomal protein S4, conserved site / WD40-repeat-containing domain / Eukaryotic translation initiation factor 3 subunit E / Armadillo-type fold / Translation initiation factor 3, subunit 12, N-terminal, eukaryotic / Ribosomal protein S12/S23 / Ribosomal protein S10, eukaryotic/archaeal / Ubiquitin conserved site / Ribosomal protein S8 / Ribosomal protein S3, C-terminal / Ribosomal protein S17e / Ribosomal protein S14 / Ribosomal protein S8e / Ribosomal protein S4e / Translational (tr)-type GTP-binding domain / Ribosomal protein S9 / Proteasome component (PCI) domain / Ubiquitin-like domain / Ribosomal protein S3Ae / Ribosomal protein S27 / Ribosomal protein S15 / Ribosomal protein S7e / Ribosomal protein S12e / RNA recognition motif domain / Ribosomal protein S28e / Ribosomal protein S17/S11 / Ribosomal protein S5/S7 / Ribosomal protein S6e / WD40 repeat / Ribosomal protein S5/S7, eukaryotic/archaeal / K Homology domain, type 2 / Ribosomal protein S19A/S15e / Ribosomal protein S4/S9, eukaryotic/archaeal / Ribosomal protein S2, eukaryotic/archaeal / Ribosomal protein S3, eukaryotic/archaeal / Ribosomal protein S23, eukaryotic/archaeal / Plectin/S10, N-terminal / Ribosomal protein S25 / Translation elongation factor EFTu-like, domain 2 / Ribosomal protein L7Ae/L30e/S12e/Gadd45 / Ribosomal protein S10 / RNA-binding S4 domain / Ribosomal protein S27a / Ribosomal protein S19/S15 / Ribosomal protein S24e / Ribosomal protein S11 / Ribosomal protein S4/S9, N-terminal / Ribosomal protein S13 / Ribosomal protein S2 / WD40 repeat, conserved site / Ribosomal protein S8e, conserved site / Ubiquitin domain / PCI domain / 40S ribosomal protein S4 C-terminus / Ribosomal family S4e / KOW motif / Ribosomal protein S9/S16 / Ribosomal_S17 N-terminal / Ribosomal protein S17 / CSN8/PSMD8/EIF3K family / eIF3 subunit 6 N terminal domain / Initiation factor eIF2 gamma, GTP-binding domain / S4 domain / Initiation factor eIF2 gamma, domain 2
Eukaryotic translation initiation factor 3 subunit M / 40S ribosomal protein S5 / 40S ribosomal protein S8 / 40S ribosomal protein S7 / 40S ribosomal protein S3a / 40S ribosomal protein S20 / Eukaryotic translation initiation factor 3 subunit E / 40S ribosomal protein S10 / 40S ribosomal protein S9 / 40S ribosomal protein S16 ...Eukaryotic translation initiation factor 3 subunit M / 40S ribosomal protein S5 / 40S ribosomal protein S8 / 40S ribosomal protein S7 / 40S ribosomal protein S3a / 40S ribosomal protein S20 / Eukaryotic translation initiation factor 3 subunit E / 40S ribosomal protein S10 / 40S ribosomal protein S9 / 40S ribosomal protein S16 / 40S ribosomal protein S27 / Eukaryotic translation initiation factor 2 subunit 3 / 40S ribosomal protein S12 / Eukaryotic translation initiation factor 4B / 40S ribosomal protein S3 / 40S ribosomal protein S17 / 40S ribosomal protein S15a / 40S ribosomal protein S14 / Eukaryotic translation initiation factor 3 subunit K / 40S ribosomal protein S25 / Eukaryotic translation initiation factor 3 subunit L / gb:174924: / Receptor of activated protein C kinase 1 / Ubiquitin-40S ribosomal protein S27a / 40S ribosomal protein S30 / 40S ribosomal protein S28 / 40S ribosomal protein S24 / 40S ribosomal protein S23 / 40S ribosomal protein S15 / 40S ribosomal protein S6 / 40S ribosomal protein S4, X isoform / 40S ribosomal protein S11 / 40S ribosomal protein S13 / 40S ribosomal protein S29 / 40S ribosomal protein S18 / 40S ribosomal protein SA
Biological speciesHomo sapiens (human)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 6.3 Å
AuthorsSchaffitzel, C. / Schaffitzel, C.
Funding support Belgium, 2items
OrganizationGrant numberCountry
European Research Council281331 Belgium
EMBL-RFBR15-54-74001 Belgium
CitationJournal: Nucleic Acids Res / Year: 2018
Title: Structure of a human cap-dependent 48S translation pre-initiation complex.
Authors: Boris Eliseev / Lahari Yeramala / Alexander Leitner / Manikandan Karuppasamy / Etienne Raimondeau / Karine Huard / Elena Alkalaeva / Ruedi Aebersold / Christiane Schaffitzel /
Abstract: Eukaryotic translation initiation is tightly regulated, requiring a set of conserved initiation factors (eIFs). Translation of a capped mRNA depends on the trimeric eIF4F complex and eIF4B to load ...Eukaryotic translation initiation is tightly regulated, requiring a set of conserved initiation factors (eIFs). Translation of a capped mRNA depends on the trimeric eIF4F complex and eIF4B to load the mRNA onto the 43S pre-initiation complex comprising 40S and initiation factors 1, 1A, 2, 3 and 5 as well as initiator-tRNA. Binding of the mRNA is followed by mRNA scanning in the 48S pre-initiation complex, until a start codon is recognised. Here, we use a reconstituted system to prepare human 48S complexes assembled on capped mRNA in the presence of eIF4B and eIF4F. The highly purified h-48S complexes are used for cross-linking/mass spectrometry, revealing the protein interaction network in this complex. We report the electron cryo-microscopy structure of the h-48S complex at 6.3 Å resolution. While the majority of eIF4B and eIF4F appear to be flexible with respect to the ribosome, additional density is detected at the entrance of the 40S mRNA channel which we attribute to the RNA-recognition motif of eIF4B. The eight core subunits of eIF3 are bound at the 40S solvent-exposed side, as well as the subunits eIF3d, eIF3b and eIF3i. elF2 and initiator-tRNA bound to the start codon are present at the 40S intersubunit side. This cryo-EM structure represents a molecular snap-shot revealing the h-48S complex following start codon recognition.
Validation Report
SummaryFull reportAbout validation report
History
DepositionDec 31, 2017Deposition site: PDBE / Processing site: PDBE
Revision 1.0Mar 14, 2018Provider: repository / Type: Initial release
Revision 1.1Apr 4, 2018Group: Data collection / Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.2Oct 3, 2018Group: Data collection / Refinement description / Category: computing / refine

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Structure visualization

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Assembly

Deposited unit
1: Eukaryotic translation initiation factor 3 subunit A
2: Eukaryotic translation initiation factor 3 subunit C
3: Eukaryotic translation initiation factor 3 subunit E
4: Eukaryotic translation initiation factor 3 subunit F
5: Eukaryotic translation initiation factor 3 subunit H
6: Eukaryotic translation initiation factor 3 subunit K
7: Eukaryotic translation initiation factor 3 subunit L
8: Eukaryotic translation initiation factor 3 subunit M
9: EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT D
A: 18S ribosomal RNA
F: Messenger RNA (26-MER)
G: 40S ribosomal protein S11
H: 40S ribosomal protein S16
I: 40S ribosomal protein S4, X isoform
J: 40S ribosomal protein S29
K: 40S ribosomal protein S9
L: 40S ribosomal protein S18
N: Transfer RNA (75-MER)
P: Eukaryotic translation initiation factor 2 subunit 1
Q: 40S ribosomal protein S23
R: 40S ribosomal protein S19
S: Eukaryotic translation initiation factor 2 subunit 3
U: 40S ribosomal protein S5
V: 40S ribosomal protein S30
W: 40S ribosomal protein S25
X: 40S ribosomal protein S7
Y: 40S ribosomal protein S27
Z: 40S ribosomal protein S13
a: 40S ribosomal protein S15a
b: 40S ribosomal protein S21
c: 40S ribosomal protein S2
d: EUKARYOTIC TRANSLATION INITIATION FACTOR 2 BETA SUBUNIT (eIF2-Beta)
e: 40S ribosomal protein S17
f: 40S ribosomal protein SA
g: 40S ribosomal protein S3
h: 40S ribosomal protein S20
i: 40S ribosomal protein S3a
j: 40S ribosomal protein S14
k: 40S ribosomal protein S26
l: 40S ribosomal protein S28
m: Receptor of activated protein C kinase 1
n: 40S ribosomal protein S15
o: 40S ribosomal protein S8
p: Ubiquitin-40S ribosomal protein S27a
q: 40S ribosomal protein S6
r: 40S ribosomal protein S12
s: 40S ribosomal protein S24
t: 40S ribosomal protein S10
u: Eukaryotic translation initiation factor 4B
w: Eukaryotic translation initiation factor 3 subunit B


Theoretical massNumber of molelcules
Total (without water)2,006,44050
Polymers2,006,44050
Non-polymers00
Water7,476415
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: cross-linking, h-48S pre-IC formation was confirmed by toe-printing and by cross-linking mass spectrometry.
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

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EUKARYOTIC TRANSLATION INITIATION FACTOR ... , 14 types, 14 molecules 123456789PSduw

#1: Protein Eukaryotic translation initiation factor 3 subunit A / eIF3a / Eukaryotic translation initiation factor 3 subunit 10 / eIF-3-theta / eIF3 p167 / eIF3 p180 ...eIF3a / Eukaryotic translation initiation factor 3 subunit 10 / eIF-3-theta / eIF3 p167 / eIF3 p180 / eIF3 p185


Mass: 164902.656 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)
#2: Protein Eukaryotic translation initiation factor 3 subunit C / eIF3c / Eukaryotic translation initiation factor 3 subunit 8 / eIF3 p110


Mass: 97923.547 Da / Num. of mol.: 1 / Mutation: A577Y / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: hela
#3: Protein Eukaryotic translation initiation factor 3 subunit E / eIF3e / Eukaryotic translation initiation factor 3 subunit 6 / Viral integration site protein INT-6 ...eIF3e / Eukaryotic translation initiation factor 3 subunit 6 / Viral integration site protein INT-6 homolog / eIF-3 p48


Mass: 52281.633 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: hela / References: UniProt: P60228
#4: Protein Eukaryotic translation initiation factor 3 subunit F / eIF3f / Deubiquitinating enzyme eIF3f / Eukaryotic translation initiation factor 3 subunit 5 / eIF- ...eIF3f / Deubiquitinating enzyme eIF3f / Eukaryotic translation initiation factor 3 subunit 5 / eIF-3-epsilon / eIF3 p47


Mass: 37846.730 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: Hela / References: ubiquitinyl hydrolase 1
#5: Protein Eukaryotic translation initiation factor 3 subunit H / eIF3h / Eukaryotic translation initiation factor 3 subunit 3 / eIF-3-gamma / eIF3 p40 subunit


Mass: 39952.281 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: hela
#6: Protein Eukaryotic translation initiation factor 3 subunit K / eIF3k / Eukaryotic translation initiation factor 3 subunit 12 / Muscle-specific gene M9 protein / ...eIF3k / Eukaryotic translation initiation factor 3 subunit 12 / Muscle-specific gene M9 protein / PLAC-24 / eIF-3 p25 / eIF-3 p28


Mass: 25129.709 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: hela / References: UniProt: Q9UBQ5
#7: Protein Eukaryotic translation initiation factor 3 subunit L / eIF3l / Eukaryotic translation initiation factor 3 subunit 6-interacting protein / Eukaryotic ...eIF3l / Eukaryotic translation initiation factor 3 subunit 6-interacting protein / Eukaryotic translation initiation factor 3 subunit E-interacting protein


Mass: 66804.766 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: hela / References: UniProt: Q9Y262
#8: Protein Eukaryotic translation initiation factor 3 subunit M / eIF3m / Fetal lung protein B5 / hFL-B5 / PCI domain-containing protein 1


Mass: 42555.832 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: hela / References: UniProt: Q7L2H7
#9: Protein EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT D


Mass: 42203.555 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)
#19: Protein Eukaryotic translation initiation factor 2 subunit 1 / Eukaryotic translation initiation factor 2 subunit alpha / eIF-2alpha


Mass: 30633.297 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: hela
#22: Protein Eukaryotic translation initiation factor 2 subunit 3 / Eukaryotic translation initiation factor 2 subunit gamma X / eIF-2gX


Mass: 45862.441 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: hela / References: UniProt: P41091
#32: Protein/peptide EUKARYOTIC TRANSLATION INITIATION FACTOR 2 BETA SUBUNIT (eIF2-Beta)


Mass: 2103.416 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)
#49: Protein Eukaryotic translation initiation factor 4B / eIF-4B


Mass: 72324.820 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: EIF4B / Plasmid: pFastBac_eIF4B / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: P23588
#50: Protein Eukaryotic translation initiation factor 3 subunit B / eIF3b / Eukaryotic translation initiation factor 3 subunit 9 / Prt1 homolog / hPrt1 / eIF-3-eta / ...eIF3b / Eukaryotic translation initiation factor 3 subunit 9 / Prt1 homolog / hPrt1 / eIF-3-eta / eIF3 p110 / eIF3 p116


Mass: 124402.336 Da / Num. of mol.: 1 / Mutation: D104E, Y124F / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: hela

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RNA chain , 3 types, 3 molecules AFN

#10: RNA chain 18S ribosomal RNA /


Mass: 572789.812 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: hela
#11: RNA chain Messenger RNA (26-MER)


Mass: 8238.953 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: beta globin derived / Plasmid: pET28a-MVHL-STOP2 / Production host: Escherichia coli (E. coli)
#18: RNA chain Transfer RNA (75-MER)


Mass: 24231.510 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: hela / References: GenBank: 174924

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40S ribosomal protein ... , 31 types, 31 molecules GHIJKLQRUVWXYZabcefghijklnoqrst

#12: Protein 40S ribosomal protein S11 / / Small ribosomal subunit protein uS17


Mass: 18468.826 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: hela / References: UniProt: P62280
#13: Protein 40S ribosomal protein S16 / / Small ribosomal subunit protein uS9


Mass: 15975.753 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: hela / References: UniProt: P62249
#14: Protein 40S ribosomal protein S4, X isoform / Ribosome / SCR10 / Single copy abundant mRNA protein / Small ribosomal subunit protein eS4


Mass: 29658.920 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: hela / References: UniProt: P62701
#15: Protein 40S ribosomal protein S29 / / Small ribosomal subunit protein uS14


Mass: 6364.426 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62273
#16: Protein 40S ribosomal protein S9 / / Small ribosomal subunit protein uS4


Mass: 21266.166 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: hela / References: UniProt: P46781
#17: Protein 40S ribosomal protein S18 / / Ke-3 / Ke3 / Small ribosomal subunit protein uS13


Mass: 16170.774 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: hela / References: UniProt: P62269
#20: Protein 40S ribosomal protein S23 / / Small ribosomal subunit protein uS12


Mass: 15757.587 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: hela / References: UniProt: P62266
#21: Protein 40S ribosomal protein S19 / / Small ribosomal subunit protein eS19


Mass: 15812.286 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: hela
#23: Protein 40S ribosomal protein S5 / / Small ribosomal subunit protein uS7


Mass: 21525.941 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: hela / References: UniProt: P46782
#24: Protein 40S ribosomal protein S30 / / Small ribosomal subunit protein eS30


Mass: 6741.048 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: hela / References: UniProt: P62861
#25: Protein 40S ribosomal protein S25 / / Small ribosomal subunit protein eS25


Mass: 8526.119 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: hela / References: UniProt: P62851
#26: Protein 40S ribosomal protein S7 / / Small ribosomal subunit protein eS7


Mass: 21716.387 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: hela / References: UniProt: P62081
#27: Protein 40S ribosomal protein S27 / / Metallopan-stimulin 1 / MPS-1 / Small ribosomal subunit protein eS27


Mass: 9480.186 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: hela / References: UniProt: P42677
#28: Protein 40S ribosomal protein S13 / / Small ribosomal subunit protein uS15


Mass: 17128.191 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: hela / References: UniProt: P62277
#29: Protein 40S ribosomal protein S15a / / Small ribosomal subunit protein uS8


Mass: 14734.357 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62244
#30: Protein 40S ribosomal protein S21 / / Small ribosomal subunit protein eS21


Mass: 8896.102 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: hela
#31: Protein 40S ribosomal protein S2 / / 40S ribosomal protein S4 / Protein LLRep3 / Small ribosomal subunit protein uS5


Mass: 24814.285 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: hela
#33: Protein 40S ribosomal protein S17 / / Small ribosomal subunit protein eS17


Mass: 14578.988 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: hela / References: UniProt: P08708
#34: Protein 40S ribosomal protein SA / / 37 kDa laminin receptor precursor / 37LRP / 37/67 kDa laminin receptor / LRP/LR / 67 kDa laminin ...37 kDa laminin receptor precursor / 37LRP / 37/67 kDa laminin receptor / LRP/LR / 67 kDa laminin receptor / 67LR / Colon carcinoma laminin-binding protein / Laminin receptor 1 / LamR / Laminin-binding protein precursor p40 / LBP/p40 / Multidrug resistance-associated protein MGr1-Ag / NEM/1CHD4 / Small ribosomal subunit protein uS2


Mass: 23360.791 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P08865
#35: Protein 40S ribosomal protein S3 / / Small ribosomal subunit protein uS3


Mass: 25158.535 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: hela
References: UniProt: P23396, DNA-(apurinic or apyrimidinic site) lyase
#36: Protein 40S ribosomal protein S20 / / Small ribosomal subunit protein uS10


Mass: 11765.890 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: hela / References: UniProt: P60866
#37: Protein 40S ribosomal protein S3a / / Small ribosomal subunit protein eS1 / v-fos transformation effector protein / Fte-1


Mass: 24944.408 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: hela / References: UniProt: P61247
#38: Protein 40S ribosomal protein S14 / / Small ribosomal subunit protein uS11


Mass: 14544.659 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: hela / References: UniProt: P62263
#39: Protein 40S ribosomal protein S26 / / Small ribosomal subunit protein eS26


Mass: 11315.428 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: hela
#40: Protein 40S ribosomal protein S28 / / Small ribosomal subunit protein eS28


Mass: 7263.394 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: hela / References: UniProt: P62857
#42: Protein 40S ribosomal protein S15 / / RIG protein / Small ribosomal subunit protein uS19


Mass: 15151.948 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: hela / References: UniProt: P62841
#43: Protein 40S ribosomal protein S8 / / Small ribosomal subunit protein eS8


Mass: 23902.871 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: hela / References: UniProt: P62241
#45: Protein 40S ribosomal protein S6 / / Phosphoprotein NP33 / Small ribosomal subunit protein eS6


Mass: 27471.535 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: hela / References: UniProt: P62753
#46: Protein 40S ribosomal protein S12 / / Small ribosomal subunit protein eS12


Mass: 13766.122 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P25398
#47: Protein 40S ribosomal protein S24 / / Small ribosomal subunit protein eS24


Mass: 15188.970 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: hela / References: UniProt: P62847
#48: Protein 40S ribosomal protein S10 / / Small ribosomal subunit protein eS10


Mass: 11773.953 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: hela / References: UniProt: P46783

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Protein , 2 types, 2 molecules mp

#41: Protein Receptor of activated protein C kinase 1 / Cell proliferation-inducing gene 21 protein / Guanine nucleotide-binding protein subunit beta-2- ...Cell proliferation-inducing gene 21 protein / Guanine nucleotide-binding protein subunit beta-2-like 1 / Guanine nucleotide-binding protein subunit beta-like protein 12.3 / Human lung cancer oncogene 7 protein / HLC-7 / Receptor for activated C kinase / Small ribosomal subunit protein RACK1


Mass: 34669.113 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: hela / References: UniProt: P63244
#44: Protein Ubiquitin-40S ribosomal protein S27a / Ubiquitin carboxyl extension protein 80


Mass: 8358.903 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: hela / References: UniProt: P62979

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Non-polymers , 1 types, 415 molecules

#51: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 415 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

Component
IDNameTypeEntity IDParent-IDSource
1human cap-dependent 48S translation pre-initiation complexRIBOSOME#1-#500MULTIPLE SOURCES
2human cap-dependent 48S translation pre-initiation complexRIBOSOME#1-#10, #12-#48, #501NATURAL
3mRNAMessenger RNACOMPLEX#111RECOMBINANT
4Eukaryotic translation initiation factor 4BCOMPLEX#491RECOMBINANT
Molecular weightValue: 2.0 MDa / Experimental value: NO
Source (natural)
IDEntity assembly-IDOrganismNcbi tax-ID
12Homo sapiens (human)9606
23Homo sapiens (human)9606
34Homo sapiens (human)9606
Source (recombinant)
IDEntity assembly-IDOrganismNcbi tax-ID
13Escherichia coli (E. coli)562
24Spodoptera frugiperda (fall armyworm)7108
Buffer solutionpH: 7.5
Details: 20 mM Tris HCl, 50 mM KOAc, 2.5 mM MgCl2, 2 mM DTT, 0.25 mM spermidine 0.25 mM GMPPNP
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid type: Quantifoil R2/2
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277 K

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELDBright-field microscopy / Nominal magnification: 112000 X / Nominal defocus max: 4000 nm / Nominal defocus min: 1500 nm
Specimen holderCryogen: NITROGEN / Model: FEI TITAN KRIOS AUTOGRID HOLDER
Image recordingElectron dose: 30 e/Å2 / Detector mode: INTEGRATING / Film or detector model: FEI FALCON II (4k x 4k)

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Processing

SoftwareName: PHENIX / Version: 1.13_2998: / Classification: refinement
EM software
IDNameVersionCategoryDetails
1EMAN2.1particle selectione2boxer.py
4CTFFIND4CTF correction
7UCSF Chimera1.1model fitting
9REFMAC5.8.0194model refinement
10RELION1.4initial Euler assignment
11RELION1.4final Euler assignment
12RELION1.4classification
13RELION1.43D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
SymmetryPoint symmetry: C1 (asymmetric)
3D reconstructionResolution: 6.3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 50604 / Algorithm: BACK PROJECTION / Num. of class averages: 1 / Symmetry type: POINT
Atomic model buildingProtocol: RIGID BODY FIT / Space: REAL / Target criteria: Cross-correlation coefficient
RefinementResolution: 6.3→270 Å / Cor.coef. Fo:Fc: 0.961 / SU B: 135.967 / SU ML: 0.877
Stereochemistry target values: MAXIMUM LIKELIHOOD WITH PHASES
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflection
Rwork0.37479 --
Obs0.37479 95026 100 %
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 105.458 Å2
Baniso -1Baniso -2Baniso -3
1-0.64 Å2-0.57 Å2-1.05 Å2
2--4.34 Å2-2.56 Å2
3----4.98 Å2
Refinement stepCycle: 1 / Total: 32425
Refine LS restraints
Refinement-IDTypeDev idealDev ideal targetNumber
ELECTRON MICROSCOPYr_bond_refined_d0.0180.01932657
ELECTRON MICROSCOPYr_bond_other_d0.0060.0229932
ELECTRON MICROSCOPYr_angle_refined_deg1.9151.95444216
ELECTRON MICROSCOPYr_angle_other_deg1.376369307
ELECTRON MICROSCOPYr_dihedral_angle_1_deg9.59253945
ELECTRON MICROSCOPYr_dihedral_angle_2_deg41.46324.4321638
ELECTRON MICROSCOPYr_dihedral_angle_3_deg20.998155854
ELECTRON MICROSCOPYr_dihedral_angle_4_deg15.94215222
ELECTRON MICROSCOPYr_chiral_restr0.150.24935
ELECTRON MICROSCOPYr_gen_planes_refined0.0090.0236132
ELECTRON MICROSCOPYr_gen_planes_other0.0050.026629
ELECTRON MICROSCOPYr_nbd_refined
ELECTRON MICROSCOPYr_nbd_other
ELECTRON MICROSCOPYr_nbtor_refined
ELECTRON MICROSCOPYr_nbtor_other
ELECTRON MICROSCOPYr_xyhbond_nbd_refined
ELECTRON MICROSCOPYr_xyhbond_nbd_other
ELECTRON MICROSCOPYr_metal_ion_refined
ELECTRON MICROSCOPYr_metal_ion_other
ELECTRON MICROSCOPYr_symmetry_vdw_refined
ELECTRON MICROSCOPYr_symmetry_vdw_other
ELECTRON MICROSCOPYr_symmetry_hbond_refined
ELECTRON MICROSCOPYr_symmetry_hbond_other
ELECTRON MICROSCOPYr_symmetry_metal_ion_refined
ELECTRON MICROSCOPYr_symmetry_metal_ion_other
ELECTRON MICROSCOPYr_mcbond_it18.67439.39615825
ELECTRON MICROSCOPYr_mcbond_other18.67339.39715824
ELECTRON MICROSCOPYr_mcangle_it32.73159.03619763
ELECTRON MICROSCOPYr_mcangle_other32.73159.03619764
ELECTRON MICROSCOPYr_scbond_it19.88336.15616832
ELECTRON MICROSCOPYr_scbond_other19.88336.15616833
ELECTRON MICROSCOPYr_scangle_it
ELECTRON MICROSCOPYr_scangle_other37.15455.10124454
ELECTRON MICROSCOPYr_long_range_B_refined63.43958918
ELECTRON MICROSCOPYr_long_range_B_other63.43958919
ELECTRON MICROSCOPYr_rigid_bond_restr
ELECTRON MICROSCOPYr_sphericity_free
ELECTRON MICROSCOPYr_sphericity_bonded
LS refinement shellResolution: 6.3→6.463 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0 0 -
Rwork0.519 7099 -
Obs--100 %

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