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- PDB-6u7h: Cryo-EM structure of the HCoV-229E spike glycoprotein -

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Basic information

Database: PDB / ID: 6u7h
TitleCryo-EM structure of the HCoV-229E spike glycoprotein
Componentsspike glycoprotein
KeywordsVIRAL PROTEIN / CoV coronavirus 229E / spike glycoprotein / APN
Function / homology
Function and homology information

host cell endoplasmic reticulum-Golgi intermediate compartment membrane / receptor-mediated virion attachment to host cell / endocytosis involved in viral entry into host cell / fusion of virus membrane with host plasma membrane / fusion of virus membrane with host endosome membrane / viral envelope / virion membrane / pathogenesis / integral component of membrane
Coronavirus S2 glycoprotein / Coronavirus S1 glycoprotein / Spike glycoprotein, Alphacoronavirus / Coronavirus S1 glycoprotein
Spike glycoprotein
Biological speciesHuman coronavirus 229E
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.1 Å
AuthorsLi, Z. / Benlekbir, S. / Rubinstein, J.L. / Rini, J.M.
Funding support Canada, 1items
OrganizationGrant numberCountry
Canadian Institutes of Health Research (CIHR) Canada
CitationJournal: Elife / Year: 2019
Title: The human coronavirus HCoV-229E S-protein structure and receptor binding.
Authors: Zhijie Li / Aidan C A Tomlinson / Alan H M Wong / Dongxia Zhou / Marc Desforges / Pierre J Talbot / Samir Benlekbir / John L Rubinstein / James M Rini /
Abstract: The coronavirus S-protein mediates receptor binding and fusion of the viral and host cell membranes. In HCoV-229E, its receptor binding domain (RBD) shows extensive sequence variation but how ...The coronavirus S-protein mediates receptor binding and fusion of the viral and host cell membranes. In HCoV-229E, its receptor binding domain (RBD) shows extensive sequence variation but how S-protein function is maintained is not understood. Reported are the X-ray crystal structures of Class III-V RBDs in complex with human aminopeptidase N (hAPN), as well as the electron cryomicroscopy structure of the 229E S-protein. The structures show that common core interactions define the specificity for hAPN and that the peripheral RBD sequence variation is accommodated by loop plasticity. The results provide insight into immune evasion and the cross-species transmission of 229E and related coronaviruses. We also find that the 229E S-protein can expose a portion of its helical core to solvent. This is undoubtedly facilitated by hydrophilic subunit interfaces that we show are conserved among coronaviruses. These interfaces likely play a role in the S-protein conformational changes associated with membrane fusion.
Validation Report
SummaryFull reportAbout validation report
DepositionSep 2, 2019Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 13, 2019Provider: repository / Type: Initial release
Revision 1.1Jan 15, 2020Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization

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Deposited unit
A: spike glycoprotein
B: spike glycoprotein
C: spike glycoprotein
hetero molecules

Theoretical massNumber of molelcules
Total (without water)398,87284

TypeNameSymmetry operationNumber
identity operation1_5551
Buried area44130 Å2
ΔGint121 kcal/mol
Surface area126000 Å2


#1: Protein/peptide spike glycoprotein

Mass: 127231.117 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Human coronavirus 229E / Strain: VR-740 / Plasmid: PB-T-PAF / Cell line (production host): HEK-293 Freestyle / Production host: Homo sapiens (human) / References: UniProt: P15423*PLUS
#2: Chemical...
ChemComp-NAG / N-ACETYL-D-GLUCOSAMINE / N-Acetylglucosamine

Mass: 221.208 Da / Num. of mol.: 63
Source method: isolated from a genetically manipulated source
Formula: C8H15NO6
#3: Chemical
ChemComp-BMA / BETA-D-MANNOSE / Mannose

Mass: 180.156 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Formula: C6H12O6
#4: Chemical
ChemComp-MAN / ALPHA-D-MANNOSE / Mannose

Mass: 180.156 Da / Num. of mol.: 12
Source method: isolated from a genetically manipulated source
Formula: C6H12O6
Has ligand of interestN

Experimental details


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

Sample preparation

ComponentName: Human coronavirus 229E spike glycoprotein / Type: COMPLEX
Details: Ectodomain generated by recombinant expression in HEK293 Freestyle cells
Entity ID: 1 / Source: RECOMBINANT
Molecular weightValue: 0.38 MDa / Experimental value: NO
Source (natural)Organism: Human coronavirus 229E
Source (recombinant)Organism: Homo sapiens (human)
Buffer solutionpH: 8
Buffer component

Buffer-ID: 1

1150 mMsodium chlorideNaClSodium chloride
210 mMTrisC4H11NO3
SpecimenConc.: 0.8 mg/ml / Details: This sample was monodisperse. / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportDetails: 15 micro Ampere / Grid material: COPPER / Grid mesh size: 400 divisions/in.
VitrificationInstrument: GATAN CRYOPLUNGE 3 / Cryogen name: ETHANE-PROPANE / Humidity: 100 % / Chamber temperature: 295 K / Details: Blot for 13 seconds before plunging

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: 75000 X / Cs: 2.7 mm
Image recordingAverage exposure time: 60 sec. / Electron dose: 42.7 e/Å2 / Detector mode: COUNTING / Film or detector model: FEI FALCON III (4k x 4k)
Image scansWidth: 4096 / Height: 4096


EM software
2EPUimage acquisition
4CTFFIND4.1.10CTF correction
7UCSF Chimera1.12model fitting
12cryoSPARC2.93D reconstruction
13PHENIX1.16RC1-3535model refinement
SymmetryPoint symmetry: C3 (3 fold cyclic)
3D reconstructionResolution: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 71350 / Symmetry type: POINT
Atomic model buildingProtocol: OTHER / Space: REAL
Details: Manual model building was done in COOT and ChimeraX/ISOLDE. A homology model based on PDB:5SZS was used as a reference during model building.
Atomic model buildingPDB-ID: 5SZS
Pdb chain-ID: A
RefinementStereochemistry target values: GeoStd + Monomer Library + CDL v1.2
Displacement parametersBiso mean: 117.43 Å2
Refine LS restraints


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