8H0Y
Structure of SARS-CoV-1 Spike Protein with Engineered x1 Disulfide (S370C and D967C), Locked-112 Conformation
8H0Y の概要
エントリーDOI | 10.2210/pdb8h0y/pdb |
EMDBエントリー | 34418 |
分子名称 | Spike glycoprotein, LINOLEIC ACID, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total) |
機能のキーワード | protein engineering, spike protein, sars-cov-1, sars-cov, viral protein |
由来する生物種 | Severe acute respiratory syndrome coronavirus |
タンパク質・核酸の鎖数 | 3 |
化学式量合計 | 422802.92 |
構造登録者 | |
主引用文献 | 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. Disulfide stabilization reveals conserved dynamic features between SARS-CoV-1 and SARS-CoV-2 spikes. Life Sci Alliance, 6:-, 2023 Cited by PubMed 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. PubMed: 37402591DOI: 10.26508/lsa.202201796 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (2.85 Å) |
構造検証レポート
検証レポート(詳細版)をダウンロード