Structure and activation mechanism of the hexameric plasma membrane H⁺-ATPase.

ABSTRACT: The S. cerevisiae plasma membrane H⁺-ATPase, Pma1, is a P3A-type ATPase and the primary protein component of the membrane compartment of Pma1 (MCP). Like other plasma membrane H⁺-ATPases, Pma1 assembles and functions as a hexamer, a property unique to this subfamily among the larger family of P-type ATPases. It has been unclear how Pma1 organizes the yeast membrane into MCP microdomains, or why it is that Pma1 needs to assemble into a hexamer to establish the membrane electrochemical proton gradient. Here we report a high-resolution cryo-EM study of native Pma1 hexamers embedded in endogenous lipids. Remarkably, we found that the Pma1 hexamer encircles a liquid-crystalline membrane domain composed of 57 ordered lipid molecules. The Pma1-encircled lipid patch structure

SUBMITTER: Zhao P 

PROVIDER: S-EPMC8575881 | biostudies-literature | 2021 Nov

REPOSITORIES: biostudies-literature