7KRS

Structural impact on SARS-CoV-2 spike protein by D614G substitution

Summary for 7KRS

• Entry DOI: 10.2210/pdb7krs/pdb
• EMDB information: 23012
• 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-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: viral protein
• Biological source: Severe acute respiratory syndrome coronavirus 2 (2019-nCoV)
• Total number of polymer chains: 3
• Total formula weight: 455422.74

Authors

Zhang, J.,Cai, Y.F.,Xiao, T.S.,Lu, J.M.,Peng, H.Q.,Sterling, S.M.,Walsh Jr, R.M.,Volloch, S.R.,Zhu, H.S.,Woosley, A.N.,Yang, W.,Sliz, P.,Chen, B. (deposition date: 2020-11-20, release date: 2021-03-24, Last modification date: 2021-05-12)

Primary citation

Zhang, J.,Cai, Y.,Xiao, T.,Lu, J.,Peng, H.,Sterling, S.M.,Walsh Jr., R.M.,Rits-Volloch, S.,Zhu, H.,Woosley, A.N.,Yang, W.,Sliz, P.,Chen, B.
Structural impact on SARS-CoV-2 spike protein by D614G substitution.
Science, 372:525-530, 2021

PubMed Abstract: Substitution for aspartic acid (D) by glycine (G) at position 614 in the spike (S) protein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) appears to facilitate rapid viral spread. The G614 strain and its recent variants are now the dominant circulating forms. Here, we report cryo-electron microscopy structures of a full-length G614 S trimer, which adopts three distinct prefusion conformations that differ primarily by the position of one receptor-binding domain. A loop disordered in the D614 S trimer wedges between domains within a protomer in the G614 spike. This added interaction appears to prevent premature dissociation of the G614 trimer-effectively increasing the number of functional spikes and enhancing infectivity-and to modulate structural rearrangements for membrane fusion. These findings extend our understanding of viral entry and suggest an improved immunogen for vaccine development.

PubMed: 33727252
DOI: 10.1126/science.abf2303

Experimental method

ELECTRON MICROSCOPY (3.2 Å)