1v9m
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
| - | |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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1v9m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v9m OCA], [http://www.ebi.ac.uk/pdbsum/1v9m PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1v9m RCSB]</span> | ||
}} | }} | ||
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[[Category: Numoto, N.]] | [[Category: Numoto, N.]] | ||
[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] | ||
| - | [[Category: GOL]] | ||
[[Category: riken structural genomics/proteomics initiative]] | [[Category: riken structural genomics/proteomics initiative]] | ||
[[Category: rsgi]] | [[Category: rsgi]] | ||
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[[Category: vov1-atpase]] | [[Category: vov1-atpase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:21:22 2008'' |
Revision as of 21:21, 30 March 2008
| |||||||
| , resolution 1.85Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | H(+)-transporting two-sector ATPase, with EC number 3.6.3.14 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
Page seeded by OCA on Mon Mar 31 00:21:22 2008
Categories: H(+)-transporting two-sector ATPase | Single protein | Thermus thermophilus | Kita, A. | Miki, K. | Numoto, N. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Riken structural genomics/proteomics initiative | Rsgi | Structural genomic | The c subunit | V-type atpase | Vov1-atpase
