6XRA

Distinct conformational states of SARS-CoV-2 spike protein

Summary for 6XRA

• Entry DOI: 10.2210/pdb6xra/pdb
• EMDB information: 22293
• Descriptor: Spike glycoprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 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: 446077.65

Authors

Zhang, J.,Cai, Y.F.,Xiao, T.S.,Peng, H.Q.,Sterling, S.M.,Walsh Jr, R.M.,Rawson, S.,Rits-Volloch, S.,Chen, B. (deposition date: 2020-07-11, release date: 2020-07-22, Last modification date: 2024-10-30)

Primary citation

Cai, Y.,Zhang, J.,Xiao, T.,Peng, H.,Sterling, S.M.,Walsh Jr., R.M.,Rawson, S.,Rits-Volloch, S.,Chen, B.
Distinct conformational states of SARS-CoV-2 spike protein.
Science, 369:1586-1592, 2020

PubMed Abstract: Intervention strategies are urgently needed to control the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) pandemic. The trimeric viral spike (S) protein catalyzes fusion between viral and target cell membranes to initiate infection. Here, we report two cryo-electron microscopy structures derived from a preparation of the full-length S protein, representing its prefusion (2.9-angstrom resolution) and postfusion (3.0-angstrom resolution) conformations, respectively. The spontaneous transition to the postfusion state is independent of target cells. The prefusion trimer has three receptor-binding domains clamped down by a segment adjacent to the fusion peptide. The postfusion structure is strategically decorated by N-linked glycans, suggesting possible protective roles against host immune responses and harsh external conditions. These findings advance our understanding of SARS-CoV-2 entry and may guide the development of vaccines and therapeutics.

PubMed: 32694201
DOI: 10.1126/science.abd4251

Experimental method

ELECTRON MICROSCOPY (3 Å)