8YG8
The early intermediate structure of baculovirus fusion protein GP64
8YG8 の概要
エントリーDOI | 10.2210/pdb8yg8/pdb |
EMDBエントリー | 39238 |
関連するBIRD辞書のPRD_ID | PRD_900017 |
分子名称 | Major envelope glycoprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total) |
機能のキーワード | structural protein |
由来する生物種 | Autographa californica nucleopolyhedrovirus |
タンパク質・核酸の鎖数 | 3 |
化学式量合計 | 163447.85 |
構造登録者 | |
主引用文献 | Guo, J.,Li, S.,Bai, L.,Zhao, H.,Shang, W.,Zhong, Z.,Maimaiti, T.,Gao, X.,Ji, N.,Chao, Y.,Li, Z.,Du, D. Structural transition of GP64 triggered by a pH-sensitive multi-histidine switch. Nat Commun, 15:7668-7668, 2024 Cited by PubMed Abstract: The fusion of viruses with cellular membranes is a critical step in the life cycle of enveloped viruses. This process is facilitated by viral fusion proteins, many of which are conformationally pH-sensitive. The specifics of how changes in pH initiate this fusion have remained largely elusive. This study presents the cryo-electron microscopy (cryo-EM) structures of a prototype class III fusion protein, GP64, in its prefusion and early intermediate states, revealing the structural intermediates accompanying the membrane fusion process. The structures identify the involvement of a pH-sensitive switch, comprising H23, H245, and H304, in sensing the low pH that triggers the initial step of membrane fusion. The pH sensing role of this switch is corroborated by assays of cell-cell syncytium formation and dual dye-labeling. The findings demonstrate that coordination between multiple histidine residues acts as a pH sensor and activator. The involvement of a multi-histidine switch in viral fusion is applicable to fusogens of human-infecting thogotoviruses and other viruses, which could lead to strategies for developing anti-viral therapies and vaccines. PubMed: 39227374DOI: 10.1038/s41467-024-51799-4 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (2.97 Å) |
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