1r5z
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(New page: 200px<br /><applet load="1r5z" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r5z, resolution 1.95Å" /> '''Crystal Structure of...)
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Revision as of 23:10, 20 November 2007
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Crystal Structure of Subunit C of V-ATPase
Overview
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.
About this Structure
1R5Z is a Single protein structure of sequence from Thermus thermophilus. Active as H(+)-transporting two-sector ATPase, with EC number 3.6.3.14 Full crystallographic information is available from OCA.
Reference
Crystal structure of a central stalk subunit C and reversible association/dissociation of vacuole-type ATPase., Iwata M, Imamura H, Stambouli E, Ikeda C, Tamakoshi M, Nagata K, Makyio H, Hankamer B, Barber J, Yoshida M, Yokoyama K, Iwata S, Proc Natl Acad Sci U S A. 2004 Jan 6;101(1):59-64. Epub 2003 Dec 18. PMID:14684831
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