1r5z: Difference between revisions
New page: left|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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[[Image:1r5z.jpg|left|200px]]<br /><applet load="1r5z" size=" | [[Image:1r5z.jpg|left|200px]]<br /><applet load="1r5z" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1r5z, resolution 1.95Å" /> | caption="1r5z, resolution 1.95Å" /> | ||
'''Crystal Structure of Subunit C of V-ATPase'''<br /> | '''Crystal Structure of Subunit C of V-ATPase'''<br /> | ||
==Overview== | ==Overview== | ||
The vacuole-type ATPases (V-ATPases) exist in various intracellular | 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== | ==About this Structure== | ||
1R5Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Active as [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] Full crystallographic information is available from [http:// | 1R5Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R5Z OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: alpha-helix]] | [[Category: alpha-helix]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:47:26 2008'' | ||
Revision as of 12:47, 21 February 2008
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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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