Structure of a lipid-bound viral membrane assembly protein reveals a modality for enclosing the lipid bilayer.

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.

SUBMITTER: Pathak PK 

PROVIDER: S-EPMC6142198 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature