1r5z
From Proteopedia
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| - | [[Image:1r5z.jpg|left|200px]] | + | [[Image:1r5z.jpg|left|200px]] |
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| - | '''Crystal Structure of Subunit C of V-ATPase''' | + | {{Structure |
| + | |PDB= 1r5z |SIZE=350|CAPTION= <scene name='initialview01'>1r5z</scene>, resolution 1.95Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal Structure of Subunit C of V-ATPase''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1R5Z is a [ | + | 1R5Z is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R5Z OCA]. |
==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:// | + | 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: H(+)-transporting two-sector ATPase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: alpha-helix]] | [[Category: alpha-helix]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:47:18 2008'' |
Revision as of 11:47, 20 March 2008
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| , resolution 1.95Å | |||||||
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| Activity: | H(+)-transporting two-sector ATPase, with EC number 3.6.3.14 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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