1u7l
From Proteopedia
Line 1: | Line 1: | ||
[[Image:1u7l.jpg|left|200px]] | [[Image:1u7l.jpg|left|200px]] | ||
- | + | <!-- | |
- | + | The line below this paragraph, containing "STRUCTURE_1u7l", creates the "Structure Box" on the page. | |
- | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
- | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
- | + | or leave the SCENE parameter empty for the default display. | |
- | | | + | --> |
- | | | + | {{STRUCTURE_1u7l| PDB=1u7l | SCENE= }} |
- | + | ||
- | + | ||
- | }} | + | |
'''Crystal Structure of subunit C (vma5p) of the yeast V-ATPase''' | '''Crystal Structure of subunit C (vma5p) of the yeast V-ATPase''' | ||
Line 23: | Line 20: | ||
==Reference== | ==Reference== | ||
Crystal structure of yeast V-ATPase subunit C reveals its stator function., Drory O, Frolow F, Nelson N, EMBO Rep. 2004 Dec;5(12):1148-52. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15540116 15540116] | Crystal structure of yeast V-ATPase subunit C reveals its stator function., Drory O, Frolow F, Nelson N, EMBO Rep. 2004 Dec;5(12):1148-52. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15540116 15540116] | ||
- | [[Category: H(+)-transporting two-sector ATPase]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
Line 29: | Line 25: | ||
[[Category: Frolow, F.]] | [[Category: Frolow, F.]] | ||
[[Category: Nelson, N.]] | [[Category: Nelson, N.]] | ||
- | [[Category: | + | [[Category: Hydrolase]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:51:32 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 07:51, 3 May 2008
Crystal Structure of subunit C (vma5p) of the yeast V-ATPase
Overview
Vacuolar H(+)-ATPase (V-ATPase) has a crucial role in the vacuolar system of eukaryotic cells. It provides most of the energy required for transport systems that utilize the proton-motive force that is generated by ATP hydrolysis. Some, but not all, of the V-ATPase subunits are homologous to those of F-ATPase and the nonhomologous subunits determine the unique features of V-ATPase. We determined the crystal structure of V-ATPase subunit C (Vma5p), which does not show any homology with F-ATPase subunits, at 1.75 A resolution. The structural features suggest that subunit C functions as a flexible stator that holds together the catalytic and membrane sectors of the enzyme. A second crystal form that was solved at 2.9 A resolution supports the flexible nature of subunit C. These structures provide a framework for exploring the unique mechanistic features of V-ATPases.
About this Structure
1U7L is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Crystal structure of yeast V-ATPase subunit C reveals its stator function., Drory O, Frolow F, Nelson N, EMBO Rep. 2004 Dec;5(12):1148-52. PMID:15540116 Page seeded by OCA on Sat May 3 10:51:32 2008