EMD-34426

Single-particle
3.35534 Å
EMD-34426 Deposition: 30/09/2022
Map released: 09/11/2022
Last modified: 23/10/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-34426

Structure of SARS-CoV-1 Spike Protein (S/native) at pH 5.5, Open Conformation

EMD-34426

Single-particle
3.35534 Å
EMD-34426 Deposition: 30/09/2022
Map released: 09/11/2022
Last modified: 23/10/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Severe acute respiratory syndrome coronavirus
Sample: SARS-CoV-1 spike protein
Fitted models: 8h16 (Avg. Q-score: 0.541)

Deposition Authors: Zhang X , Li Z, Liu Y , Wang J, Fu L, Wang P, He J , Xiong X
Disulfide stabilization reveals conserved dynamic features between SARS-CoV-1 and SARS-CoV-2 spikes.
Zhang X , Li Z, Zhang Y, Liu Y , Wang J, Liu B, Chen Q, Wang Q, Fu L, Wang P, Zhong X, Jin L, Yan Q, Chen L, He J , Zhao J, Xiong X
(2023) Life Sci Alliance , 6
PUBMED: 37402591
DOI: doi:10.26508/lsa.202201796
ISSN: 2575-1077
Abstract:
SARS-CoV-2 spike protein (S) is structurally dynamic and has been observed by cryo-EM to adopt a variety of prefusion conformations that can be categorized as locked, closed, and open. S-trimers adopting locked conformations are tightly packed featuring structural elements incompatible with RBD in the "up" position. For SARS-CoV-2 S, it has been shown that the locked conformations are transient under neutral pH. Probably because of their transience, locked conformations remain largely uncharacterized for SARS-CoV-1 S. In this study, we introduced x1, x2, and x3 disulfides into SARS-CoV-1 S. Some of these disulfides have been shown to preserve rare locked conformations when introduced to SARS-CoV-2 S. Introduction of these disulfides allowed us to image a variety of locked and other rare conformations for SARS-CoV-1 S by cryo-EM. We identified bound cofactors and structural features that are associated with SARS-CoV-1 S locked conformations. We compare newly determined structures with other available spike structures of SARS-related CoVs to identify conserved features and discuss their possible functions.