EMD-34425
Structure of SARS-CoV-1 Spike Protein (S/native) at pH 5.5, Closed Conformation
EMD-34425
Single-particle3.14182 Å
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Map released: 09/11/2022
Last modified: 20/11/2024
Sample Organism:
Severe acute respiratory syndrome coronavirus
Sample: SARS-CoV-1 spike protein
Fitted models: 8h15 (Avg. Q-score: 0.578)
Deposition Authors: Zhang X
,
Li Z,
Liu Y
,
Wang J,
Fu L,
Wang P,
He J
,
Xiong X
Sample: SARS-CoV-1 spike protein
Fitted models: 8h15 (Avg. Q-score: 0.578)
Deposition Authors: Zhang X
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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
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(2023) Life Sci Alliance , 6
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.
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.