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Crystal structure of a central stalk subunit C and reversible association/dissociation of vacuole-type ATPase.

ABSTRACT: 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 V(1) (soluble) and the V(o) (membrane bound) domains. Subunit C, attached to the V(o) domain, seems to have a socket like function in attaching the central-stalk subunits of the V(1) domain. This architecture seems essential for the reversible association/dissociation of the V(1) and the V(o) domains, unique for V-ATPase activity regulation.

SUBMITTER: Iwata M 

PROVIDER: S-EPMC314138 | biostudies-literature | 2004 Jan

REPOSITORIES: biostudies-literature

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Crystal structure of a central stalk subunit C and reversible association/dissociation of vacuole-type ATPase.

Iwata Momi M   Imamura Hiromi H   Stambouli Elizabeth E   Ikeda Chiyo C   Tamakoshi Masatada M   Nagata Koji K   Makyio Hisayoshi H   Hankamer Ben B   Barber Jim J   Yoshida Masasuke M   Yokoyama Ken K   Iwata So S  

Proceedings of the National Academy of Sciences of the United States of America 20031218 1

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 resu  ...[more]

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