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- PDB-5w9i: MERS S ectodomain trimer in complex with variable domain of neutr... -

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Database: PDB / ID: 5w9i
TitleMERS S ectodomain trimer in complex with variable domain of neutralizing antibody G4
  • G4 VH
  • G4 VL
  • Spike glycoprotein
KeywordsVIRAL PROTEIN / Immunogen / peplomer / viral spike / MERS / MERS S protein / antibody / G4
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 / pathogenesis / host cell plasma membrane / virion membrane / integral component of membrane
Spike receptor binding domain superfamily / Spike receptor binding domain / Coronavirus S2 glycoprotein / Spike glycoprotein / Coronavirus S2 glycoprotein / Spike receptor binding domain / Coronovirus spike glycoprotein, heptad repeat 2 domain
Spike glycoprotein / Spike glycoprotein
Biological speciesMiddle East respiratory syndrome-related coronavirus
Mus musculus (house mouse)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.6 Å
AuthorsPallesen, J. / Ward, A.B.
Funding support United States, 2items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical SciencesP20GM113132 United States
National Institutes of Health/National Institute Of Allergy and Infectious DiseasesR01AI127521 United States
CitationJournal: Proc. Natl. Acad. Sci. U.S.A. / Year: 2017
Title: Immunogenicity and structures of a rationally designed prefusion MERS-CoV spike antigen.
Authors: Jesper Pallesen / Nianshuang Wang / Kizzmekia S Corbett / Daniel Wrapp / Robert N Kirchdoerfer / Hannah L Turner / Christopher A Cottrell / Michelle M Becker / Lingshu Wang / Wei Shi / Wing-Pui Kong / Erica L Andres / Arminja N Kettenbach / Mark R Denison / James D Chappell / Barney S Graham / Andrew B Ward / Jason S McLellan /
Abstract: Middle East respiratory syndrome coronavirus (MERS-CoV) is a lineage C betacoronavirus that since its emergence in 2012 has caused outbreaks in human populations with case-fatality rates of ∼36%. ...Middle East respiratory syndrome coronavirus (MERS-CoV) is a lineage C betacoronavirus that since its emergence in 2012 has caused outbreaks in human populations with case-fatality rates of ∼36%. As in other coronaviruses, the spike (S) glycoprotein of MERS-CoV mediates receptor recognition and membrane fusion and is the primary target of the humoral immune response during infection. Here we use structure-based design to develop a generalizable strategy for retaining coronavirus S proteins in the antigenically optimal prefusion conformation and demonstrate that our engineered immunogen is able to elicit high neutralizing antibody titers against MERS-CoV. We also determined high-resolution structures of the trimeric MERS-CoV S ectodomain in complex with G4, a stem-directed neutralizing antibody. The structures reveal that G4 recognizes a glycosylated loop that is variable among coronaviruses and they define four conformational states of the trimer wherein each receptor-binding domain is either tightly packed at the membrane-distal apex or rotated into a receptor-accessible conformation. Our studies suggest a potential mechanism for fusion initiation through sequential receptor-binding events and provide a foundation for the structure-based design of coronavirus vaccines.
Validation Report
SummaryFull reportAbout validation report
DepositionJun 23, 2017Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 16, 2017Provider: repository / Type: Initial release
Revision 1.1Aug 30, 2017Group: Database references / Category: citation / citation_author
Item: _citation.journal_abbrev / _citation.pdbx_database_id_PubMed / _citation.title
Revision 1.2Sep 13, 2017Group: Author supporting evidence / Data collection / Database references
Category: citation / em_software / pdbx_audit_support
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _em_software.name / _pdbx_audit_support.funding_organization
Revision 1.3Nov 8, 2017Group: Derived calculations / Category: pdbx_struct_assembly
Item: _pdbx_struct_assembly.details / _pdbx_struct_assembly.method_details
Revision 1.4Jul 18, 2018Group: Data collection / Experimental preparation / Category: em_sample_support / em_software / Item: _em_sample_support.grid_type / _em_software.name
Revision 1.5Nov 6, 2019Group: Data collection / Other / Category: atom_sites / cell
Item: _atom_sites.fract_transf_matrix[1][1] / _atom_sites.fract_transf_matrix[2][2] ..._atom_sites.fract_transf_matrix[1][1] / _atom_sites.fract_transf_matrix[2][2] / _atom_sites.fract_transf_matrix[3][3] / _cell.Z_PDB / _cell.length_a / _cell.length_b / _cell.length_c

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Deposited unit
A: Spike glycoprotein
B: Spike glycoprotein
C: G4 VH
D: G4 VL
E: Spike glycoprotein
F: Spike glycoprotein
G: G4 VH
H: G4 VL
I: Spike glycoprotein
J: Spike glycoprotein
K: G4 VH
L: G4 VL
hetero molecules

Theoretical massNumber of molelcules
Total (without water)1,039,43175

TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area53720 Å2
ΔGint-19 kcal/mol
Surface area163120 Å2


#1: Protein/peptide
Spike glycoprotein / S protein

Mass: 146325.969 Da / Num. of mol.: 6 / Mutation: V1060P, L1061P
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Middle East respiratory syndrome-related coronavirus
Production host: Homo sapiens (human) / References: UniProt: W5ZZF5, UniProt: K9N5Q8*PLUS
#2: Protein/peptide G4 VH

Mass: 25312.352 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Production host: Homo sapiens (human)
#3: Protein/peptide G4 VL

Mass: 23867.367 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Production host: Homo sapiens (human)
#4: Chemical...

Mass: 221.208 Da / Num. of mol.: 63
Source method: isolated from a genetically manipulated source
Formula: C8H15NO6 / N-Acetylglucosamine

Experimental details


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

Sample preparation

ComponentName: MERS S ectodomain trimer in complex with Fab of neutralizing antibody G4
Type: COMPLEX / Entity ID: 1, 2, 3, 4 / Source: MULTIPLE SOURCES
Molecular weightValue: 0.6 MDa / Experimental value: NO
Source (natural)Organism: Middle East respiratory syndrome-related coronavirus
Buffer solutionpH: 7.4
Buffer componentName: TBS
SpecimenConc.: 1 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid material: COPPER / Grid mesh size: 400 divisions/in. / Grid type: C-flat
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277 K

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: 29000 X / Nominal defocus max: 2500 nm / Nominal defocus min: 700 nm / Cs: 2.7 mm / C2 aperture diameter: 70 µm / Alignment procedure: COMA FREE
Image recordingAverage exposure time: 0.2 sec. / Electron dose: 1.89 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Num. of grids imaged: 1
Image scansSampling size: 5 µm / Movie frames/image: 35 / Used frames/image: 1-35


SoftwareName: PHENIX / Version: 1.11.1_2580: / Classification: refinement
EM software
2Leginonimage acquisition
4CTFFIND3CTF correction
7Rosettamodel fitting
9RELION1.4initial Euler assignment
10RELION1.4final Euler assignment
12RELION1.43D reconstruction
13Rosettamodel refinement
14PHENIXmodel refinement
Particle selectionNum. of particles selected: 37180
SymmetryPoint symmetry: C3 (3 fold cyclic)
3D reconstructionResolution: 3.6 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 37180 / Symmetry type: POINT
Atomic model buildingProtocol: OTHER / Space: REAL
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