7BNM

Closed conformation of D614G SARS-CoV-2 spike protein

This is a non-PDB format compatible entry.

Summary for 7BNM

• Entry DOI: 10.2210/pdb7bnm/pdb
• EMDB information: 12229
• Descriptor: Spike glycoprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• Functional Keywords: spike, sars-cov-2, viral protein
• Biological source: Severe acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2)
• Total number of polymer chains: 3
• Total formula weight: 403043.10

Authors

Benton, D.J.,Wrobel, A.G.,Rosenthal, P.B.,Gamblin, S.J. (deposition date: 2021-01-22, release date: 2021-02-03, Last modification date: 2024-11-06)

Primary citation

Benton, D.J.,Wrobel, A.G.,Roustan, C.,Borg, A.,Xu, P.,Martin, S.R.,Rosenthal, P.B.,Skehel, J.J.,Gamblin, S.J.
The effect of the D614G substitution on the structure of the spike glycoprotein of SARS-CoV-2.
Proc.Natl.Acad.Sci.USA, 118:-, 2021

PubMed Abstract: The majority of currently circulating severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) viruses have mutant spike glycoproteins that contain the D614G substitution. Several studies have suggested that spikes with this substitution are associated with higher virus infectivity. We use cryo-electron microscopy to compare G614 and D614 spikes and show that the G614 mutant spike adopts a range of more open conformations that may facilitate binding to the SARS-CoV-2 receptor, ACE2, and the subsequent structural rearrangements required for viral membrane fusion.

PubMed: 33579792
DOI: 10.1073/pnas.2022586118

Experimental method

ELECTRON MICROSCOPY (3.6 Å)