6CB6

CRYSTAL STRUCTURE OF VACCINIA VIRUS A6 N-TERMINUS (SPACE GROUP C2)

6CB6 の概要

• エントリーDOI: 10.2210/pdb6cb6/pdb
• 関連するPDBエントリー: 4X3W
• 分子名称: Protein A6 (2 entities in total)
• 機能のキーワード: vaccinia virus, a6, poxviruses, virion core protein, virion morphogenesis, viral protein
• 由来する生物種: Vaccinia virus (strain Copenhagen) (VACV)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14377.60

構造登録者

Han, Y.,Zhang, B.,Deng, J. (登録日: 2018-02-02, 公開日: 2018-12-12, 最終更新日: 2024-10-23)

主引用文献

Pathak, P.K.,Peng, S.,Meng, X.,Han, Y.,Zhang, B.,Zhang, F.,Xiang, Y.,Deng, J.
Structure of a lipid-bound viral membrane assembly protein reveals a modality for enclosing the lipid bilayer.
Proc. Natl. Acad. Sci. U.S.A., 115:7028-7032, 2018

PubMed Abstract: Cellular membranes are maintained as closed compartments, broken up only transiently during membrane reorganization or lipid transportation. However, open-ended membranes, likely derived from scissions of the endoplasmic reticulum, persist in vaccinia virus-infected cells during the assembly of the viral envelope. A group of viral membrane assembly proteins (VMAPs) were identified as essential for this process. To understand the mechanism of VMAPs, we determined the 2.2-Å crystal structure of the largest member, named A6, which is a soluble protein with two distinct domains. The structure of A6 displays a novel protein fold composed mainly of alpha helices. The larger C-terminal domain forms a unique cage that encloses multiple glycerophospholipids with a lipid bilayer-like configuration. The smaller N-terminal domain does not bind lipid but negatively affects lipid binding by A6. Mutations of key hydrophobic residues lining the lipid-binding cage disrupt lipid binding and abolish viral replication. Our results reveal a protein modality for enclosing the lipid bilayer and provide molecular insight into a viral machinery involved in generating and/or stabilizing open-ended membranes.

PubMed: 29915071
DOI: 10.1073/pnas.1805855115

実験手法

X-RAY DIFFRACTION (1.8 Å)