1r5z
From Proteopedia
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'''Crystal Structure of Subunit C of V-ATPase''' | '''Crystal Structure of Subunit C of V-ATPase''' | ||
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==Reference== | ==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:[http://www.ncbi.nlm.nih.gov/pubmed/14684831 14684831] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/14684831 14684831] | ||
| - | [[Category: H(+)-transporting two-sector ATPase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermus thermophilus]] | [[Category: Thermus thermophilus]] | ||
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[[Category: Yokoyama, K.]] | [[Category: Yokoyama, K.]] | ||
[[Category: Yoshida, M.]] | [[Category: Yoshida, M.]] | ||
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Revision as of 04:07, 3 May 2008
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. 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 Page seeded by OCA on Sat May 3 07:07:23 2008
