期刊
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
卷 1757, 期 5-6, 页码 297-303出版社
ELSEVIER
DOI: 10.1016/j.bbabio.2006.03.011
关键词
V-ATPase; subunit C; 3D structure; mechanism; conformation
V-ATPase is a multi-subunit membrane protein complex, it translocates protons across biological membranes, generating electrical and pH gradients which are used for varieties of cellular processes. V-ATPase is composed of two distinct sub-complexes: a membrane bound V-0 subcomplex, composed of 6 different subunits, which is responsible for proton transport and a soluble cytosolic facing V-1 sub-complex, composed of 8 different subunits which hydrolyse ATP. The two sub-complexes are held together via a flexible stator. One of the main features of eukaryotic V-ATPase is its ability to reversibly dissociate to its sub-complexes in response to changing cellular conditions, which arrest both proton translocation and ATP hydrolysis, suggesting a regulation function. Subunit C (vma5p in yeast) was shown by several biochemical, genetic and recent structural data to function as a flexible stator holding the two sectors of the complex together and regulating the reversible association/dissociation of the complex, partly via association with F-actin filaments. Structural features of subunit C that allow smooth energy conversion and interaction with actin and nucleotides are discussed. (c) 2006 Elsevier B.V. All rights reserved.
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