期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：2004
卷号：101
期号：1
页码：59-64
DOI：10.1073/pnas.0305165101
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：The vacuole-type ATPases (V-ATPases) exist in various intracellular compartments of eukaryotic cells to regulate physiological processes by controlling the acidic environment. The crystal structure of the subunit C of Thermus thermophilus V-ATPase, homologous to eukaryotic subunit d of V-ATPases, has been determined at 1.95-A resolution and located into the holoenzyme complex structure obtained by single particle analysis as suggested by the results of subunit cross-linking experiments. The result shows that V-ATPase is substantially longer than the related F-type ATPase, due to the insertion of subunit C between the V1 (soluble) and the Vo (membrane bound) domains. Subunit C, attached to the Vo domain, seems to have a socket like function in attaching the central-stalk subunits of the V1 domain. This architecture seems essential for the reversible association/dissociation of the V1 and the Vo domains, unique for V-ATPase activity regulation.
