6BR9

Structure of A6 reveals a novel lipid transporter

6BR9 の概要

• エントリーDOI: 10.2210/pdb6br9/pdb
• 分子名称: Protein A6 homolog, [(2~{R})-1-[2-azanylethoxy(oxidanyl)phosphoryl]oxy-3-hexadecanoyloxy-propan-2-yl] (~{Z})-octadec-9-enoate, (1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL (11E)-OCTADEC-11-ENOATE, ... (4 entities in total)
• 機能のキーワード: poxvirus, a6, lipid binding, membrane biogenesis, lipid binding protein
• 由来する生物種: Fowlpox virus (strain NVSL) (FPV)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 45352.78

構造登録者

Deng, J.,Peng, S.,Pathak, P. (登録日: 2017-11-30, 公開日: 2018-06-20, 最終更新日: 2024-03-13)

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 (2.2 Å)