1R5Z

Crystal Structure of Subunit C of V-ATPase

Summary for 1R5Z

• Entry DOI: 10.2210/pdb1r5z/pdb
• Descriptor: V-type ATP synthase subunit C (2 entities in total)
• Functional Keywords: alpha-helix, hydrolase
• Biological source: Thermus thermophilus
• Total number of polymer chains: 3
• Total formula weight: 107905.71

Authors

Iwata, M.,Imamura, H.,Stambouli, E.,Ikeda, C.,Tamakoshi, M.,Nagata, K.,Makyio, H.,Hankamer, B.,Barber, J.,Yoshida, M.,Yokoyama, K.,Iwata, S. (deposition date: 2003-10-14, release date: 2004-01-13, Last modification date: 2024-11-13)

Primary citation

Iwata, M.,Imamura, H.,Stambouli, E.,Ikeda, C.,Tamakoshi, M.,Nagata, K.,Makyio, H.,Hankamer, B.,Barber, J.,Yoshida, M.,Yokoyama, K.,Iwata, S.
Crystal structure of a central stalk subunit C and reversible association/dissociation of vacuole-type ATPase.
Proc.Natl.Acad.Sci.Usa, 101:59-64, 2004

PubMed 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.

PubMed: 14684831
DOI: 10.1073/pnas.0305165101

Experimental method

X-RAY DIFFRACTION (1.95 Å)