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1v9m

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[[Image:1v9m.jpg|left|200px]]<br /><applet load="1v9m" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1v9m.jpg|left|200px]]
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caption="1v9m, resolution 1.85&Aring;" />
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'''Crystal structure of the C subunit of V-type ATPase from Thermus thermophilus'''<br />
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{{Structure
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|PDB= 1v9m |SIZE=350|CAPTION= <scene name='initialview01'>1v9m</scene>, resolution 1.85&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|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]
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|GENE=
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}}
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'''Crystal structure of the C subunit of V-type ATPase from Thermus thermophilus'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1V9M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1V9M OCA].
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1V9M 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=1V9M OCA].
==Reference==
==Reference==
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Structure of the C subunit of V-type ATPase from Thermus thermophilus at 1.85 A resolution., Numoto N, Kita A, Miki K, Acta Crystallogr D Biol Crystallogr. 2004 May;60(Pt 5):810-5. Epub 2004, Apr 21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15103125 15103125]
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Structure of the C subunit of V-type ATPase from Thermus thermophilus at 1.85 A resolution., Numoto N, Kita A, Miki K, Acta Crystallogr D Biol Crystallogr. 2004 May;60(Pt 5):810-5. Epub 2004, Apr 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15103125 15103125]
[[Category: H(+)-transporting two-sector ATPase]]
[[Category: H(+)-transporting two-sector ATPase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: riken structural genomics/proteomics initiative]]
[[Category: riken structural genomics/proteomics initiative]]
[[Category: rsgi]]
[[Category: rsgi]]
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[[Category: structural genomics]]
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[[Category: structural genomic]]
[[Category: the c subunit]]
[[Category: the c subunit]]
[[Category: thermus thermophilus]]
[[Category: thermus thermophilus]]
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[[Category: vov1-atpase]]
[[Category: vov1-atpase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:33:05 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:42:42 2008''

Revision as of 12:42, 20 March 2008


PDB ID 1v9m

Drag the structure with the mouse to rotate
, resolution 1.85Å
Ligands:
Activity: H(+)-transporting two-sector ATPase, with EC number 3.6.3.14
Coordinates: save as pdb, mmCIF, xml



Crystal structure of the C subunit of V-type ATPase from Thermus thermophilus


Overview

The V-type H(+)-ATPases are similar to the F-type ATP synthases in their structure and functional mechanism. They hydrolyze ATP coupled with proton translocation across a membrane, but in some archaea and eubacteria they also synthesize ATP in the reverse reaction. The C subunit is one of the components of the membrane-bound V(0) moiety of V-type ATPases. The C subunit of V-type H(+)-ATPase from Thermus thermophilus was crystallized in a monoclinic form and its crystal structure was determined at 1.85 A resolution by the MAD method using selenomethionyl protein. The structure has a cone (tapered cylinder) shape consisting of only two types of helix (long and short) as secondary-structure elements. The molecule is divided into three similar domains, each of which has essentially the same topology. On the basis of the structural features and molecular-surface charge distribution, it is suggested that the bottom side of the C subunit is a possible binding site for the V(0) proteolipid L-subunit ring and that the C subunit might function as a spacer unit between the proteolipid L-subunit ring and the rotating V(1) central shaft.

About this Structure

1V9M is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.

Reference

Structure of the C subunit of V-type ATPase from Thermus thermophilus at 1.85 A resolution., Numoto N, Kita A, Miki K, Acta Crystallogr D Biol Crystallogr. 2004 May;60(Pt 5):810-5. Epub 2004, Apr 21. PMID:15103125

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