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- PDB-1tyq: Crystal structure of Arp2/3 complex with bound ATP and calcium -

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Basic information

Entry
Database: PDB / ID: 1tyq
TitleCrystal structure of Arp2/3 complex with bound ATP and calcium
Components
  • (Actin-related ...) x 2
  • (Arp2/3 complex ...) x 5
KeywordsSTRUCTURAL PROTEIN
Function / homology
Function and homology information


Arp2/3 protein complex / Arp2/3 complex-mediated actin nucleation / positive regulation of double-strand break repair via homologous recombination / positive regulation of lamellipodium assembly / cilium assembly / actin filament polymerization / cell projection / structural constituent of cytoskeleton / site of double-strand break / actin filament binding ...Arp2/3 protein complex / Arp2/3 complex-mediated actin nucleation / positive regulation of double-strand break repair via homologous recombination / positive regulation of lamellipodium assembly / cilium assembly / actin filament polymerization / cell projection / structural constituent of cytoskeleton / site of double-strand break / actin filament binding / cell migration / actin binding / neuron projection / synapse / positive regulation of transcription by RNA polymerase II / ATP binding / nucleus / cytosol / cytoplasm
Actin-related protein 2/3 complex subunit 5 superfamily / WD40 repeat / ATPase, nucleotide binding domain / Actin-related protein 2/3 complex subunit 3 superfamily / WD40-repeat-containing domain superfamily / Arp2/3 complex subunit 2/4 / Actin-related protein 2/3 complex subunit 1B / Actin/actin-like conserved site / WD40-repeat-containing domain / Actin-related protein 2/3 complex subunit 1 ...Actin-related protein 2/3 complex subunit 5 superfamily / WD40 repeat / ATPase, nucleotide binding domain / Actin-related protein 2/3 complex subunit 3 superfamily / WD40-repeat-containing domain superfamily / Arp2/3 complex subunit 2/4 / Actin-related protein 2/3 complex subunit 1B / Actin/actin-like conserved site / WD40-repeat-containing domain / Actin-related protein 2/3 complex subunit 1 / WD40/YVTN repeat-like-containing domain superfamily / Actin-related protein 3 / Actin-related protein 2/3 complex subunit 4 / Actin-related protein 2/3 complex subunit 3 / Actin-related protein 2/3 complex subunit 2 / Actin-related protein 2/3 complex subunit 5 / Actin family / Actin-related protein 2/3 complex subunit 3 / Yope Regulator; Chain: A, - #20 / Actin-related protein 2/3 complex subunit 5 / Arp2/3 complex 21 kDa subunit ARPC3 / Yope Regulator; Chain: A, / Actin; Chain A, domain 2 / Actin; Chain A, domain 2 / ATPase, substrate binding domain, subdomain 4 / Actin; Chain A, domain 4 / YVTN repeat-like/Quinoprotein amine dehydrogenase / ATPase, nucleotide binding domain / 7 Propeller / Methylamine Dehydrogenase; Chain H / Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat / Alpha Horseshoe / Nucleotidyltransferase; domain 5 / Roll / Alpha-Beta Complex / 2-Layer Sandwich / Orthogonal Bundle / Mainly Beta / Mainly Alpha / Alpha Beta
Actin-related protein 2/3 complex subunit 1B / Actin-related protein 2 / Actin-related protein 3 / Actin-related protein 2/3 complex subunit 4 / Actin-related protein 2/3 complex subunit 2 / Actin-related protein 2/3 complex subunit 5 / Actin-related protein 2/3 complex subunit 3
Biological speciesBos taurus (cattle)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.55 Å
AuthorsNolen, B.J. / Littlefield, R.S. / Pollard, T.D.
CitationJournal: Proc.Natl.Acad.Sci.Usa / Year: 2004
Title: Crystal structures of actin-related protein 2/3 complex with bound ATP or ADP
Authors: Nolen, B.J. / Littlefield, R.S. / Pollard, T.D.
Validation Report
SummaryFull reportAbout validation report
History
DepositionJul 8, 2004Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Nov 9, 2004Provider: repository / Type: Initial release
Revision 1.1Apr 30, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Actin-related protein 3
B: Actin-related Protein 2
C: Arp2/3 complex 41kDa subunit
D: Arp2/3 complex 34kDa subunit
E: Arp2/3 complex 21kDa subunit
F: Arp2/3 complex 20kDa subunit
G: Arp2/3 Complex 16kDa Subunit
hetero molecules


Theoretical massNumber of molelcules
Total (without water)225,32511
Polymers224,2317
Non-polymers1,0954
Water3,261181
1


TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area21360 Å2
ΔGint-120 kcal/mol
Surface area67910 Å2
MethodPISA
Unit cell
γ
α
β
Length a, b, c (Å)111.368, 129.392, 199.692
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

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Actin-related ... , 2 types, 2 molecules AB

#1: Protein Actin-related protein 3 / Actin-like protein 3 / Actin-2


Mass: 47428.031 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: P61157
#2: Protein Actin-related Protein 2


Mass: 44818.711 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: A7MB62*PLUS

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Arp2/3 complex ... , 5 types, 5 molecules CDEFG

#3: Protein Arp2/3 complex 41kDa subunit


Mass: 41016.738 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: Q58CQ2*PLUS
#4: Protein Arp2/3 complex 34kDa subunit


Mass: 34402.043 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: Q3MHR7*PLUS
#5: Protein Arp2/3 complex 21kDa subunit


Mass: 20572.666 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: Q3T035*PLUS
#6: Protein Arp2/3 complex 20kDa subunit


Mass: 19697.047 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: Q148J6*PLUS
#7: Protein Arp2/3 Complex 16kDa Subunit


Mass: 16295.317 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / Tissue: thymus / References: UniProt: Q3SYX9*PLUS

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Non-polymers , 3 types, 185 molecules

#8: Chemical ChemComp-CA / CALCIUM ION / Calcium


Mass: 40.078 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Ca
#9: Chemical ChemComp-ATP / ADENOSINE-5'-TRIPHOSPHATE / Adenosine triphosphate


Mass: 507.181 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H16N5O13P3 / Comment: ATP, energy-carrying molecule*YM
#10: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 181 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 3.21 Å3/Da / Density % sol: 61.7 %
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop / pH: 7.5
Details: PEG 8000, potassium thiocyanate, Hepes, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K

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Data collection

Diffraction sourceSource: SYNCHROTRON / Site: NSLS / Beamline: X9B / Wavelength: 0.97946 Å
DetectorType: MARRESEARCH / Detector: IMAGE PLATE / Date: Oct 10, 2002
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97946 Å / Relative weight: 1
ReflectionResolution: 2.55→30 Å / Num. all: 73162 / Num. obs: 72816 / % possible obs: 79.2 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Rsym value: 0.093 / Net I/σ(I): 21.4
Reflection shellResolution: 2.55→2.64 Å / Mean I/σ(I) obs: 5 / Rsym value: 0.358 / % possible all: 68.8

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Processing

Software
NameClassification
HKL-2000data collection
SCALEPACKdata scaling
CNSrefinement
HKL-2000data reduction
CNSphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1K8K
Resolution: 2.55→30 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber
RfactorNum. reflectionSelection details
Rfree0.272 3654 RANDOM
Rwork0.232 --
All0.234 72816 -
Obs0.234 72816 -
Refinement stepCycle: LAST / Resolution: 2.55→30 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms13341 0 64 181 13586
Refine LS restraints
Refinement-IDTypeDev ideal
X-RAY DIFFRACTIONc_angle_deg1.28
X-RAY DIFFRACTIONc_bond_d0.007

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