1u7l
From Proteopedia
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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 with TLA as ligand. 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 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
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