PDBsum entry 7mjh

Viral protein

PDB id: 7mjh

Contents

Protein chains

1040 a.a.

125 a.a.

Ligands

NAG-NAG ×18

NAG ×24

PDB id:

7mjh

Name:

Viral protein

Title:

Cryo-em structure of the sars-cov-2 n501y mutant spike protein ectodomain bound to vh ab8

Structure:

Spike glycoprotein. Chain: a, b, c. Synonym: s glycoprotein,e2,peplomer protein. Engineered: yes. Mutation: yes. Vh ab8. Chain: d, e, f. Engineered: yes

Source:

Severe acute respiratory syndrome coronavirus 2. 2019-ncov, sars-cov-2. Organism_taxid: 2697049. Gene: s, 2. Expressed in: homo sapiens. Expression_system_taxid: 9606. Synthetic construct. Organism_taxid: 32630.

Authors:

X.Zhu,D.Mannar,S.S.Srivastava,A.M.Berezuk,J.P.Demers,J.W.Saville, K.Leopold,W.Li,D.S.Dimitrov,K.S.Tuttle,S.Zhou,S.Chittori, S.Subramaniam

Key ref:

X.Zhu et al. (2021). Cryo-electron microscopy structures of the N501Y SARS-CoV-2 spike protein in complex with ACE2 and 2 potent neutralizing antibodies. PLoS Biol, 19, e3001237. PubMed id: 33914735 DOI: 10.1371/journal.pbio.3001237

Date:

20-Apr-21 Release date: 12-May-21

Protein chains

P0DTC2  (SPIKE_SARS2) -  Spike glycoprotein from Severe acute respiratory syndrome coronavirus 2

Seq: 1273 a.a.

Struc: 1040 a.a.*

Protein chains

No UniProt id for this chain

Struc: 125 a.a.

* PDB and UniProt seqs differ at 7 residue positions (black crosses)

DOI no: 10.1371/journal.pbio.3001237

PLoS Biol 19:e3001237 (2021)

PubMed id: 33914735

Cryo-electron microscopy structures of the N501Y SARS-CoV-2 spike protein in complex with ACE2 and 2 potent neutralizing antibodies.

X.Zhu, D.Mannar, S.S.Srivastava, A.M.Berezuk, J.P.Demers, J.W.Saville, K.Leopold, W.Li, D.S.Dimitrov, K.S.Tuttle, S.Zhou, S.Chittori, S.Subramaniam.

ABSTRACT

The recently reported "UK variant" (B.1.1.7) of SARS-CoV-2 is thought to be more infectious than previously circulating strains as a result of several changes, including the N501Y mutation. We present a 2.9-Å resolution cryo-electron microscopy (cryo-EM) structure of the complex between the ACE2 receptor and N501Y spike protein ectodomains that shows Y501 inserted into a cavity at the binding interface near Y41 of ACE2. This additional interaction provides a structural explanation for the increased ACE2 affinity of the N501Y mutant, and likely contributes to its increased infectivity. However, this mutation does not result in large structural changes, enabling important neutralization epitopes to be retained in the spike receptor binding domain. We confirmed this through biophysical assays and by determining cryo-EM structures of spike protein ectodomains bound to 2 representative potent neutralizing antibody fragments.