1U7L

Crystal Structure of subunit C (vma5p) of the yeast V-ATPase

Summary for 1U7L

• Entry DOI: 10.2210/pdb1u7l/pdb
• Descriptor: Vacuolar ATP synthase subunit C, L(+)-TARTARIC ACID (3 entities in total)
• Functional Keywords: hydrolase, structural protein
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Vacuole membrane; Peripheral membrane protein: P31412
• Total number of polymer chains: 1
• Total formula weight: 44391.44

Authors

Nelson, N.,Frolow, F.,Drory, O. (deposition date: 2004-08-04, release date: 2004-11-23, Last modification date: 2024-03-20)

Primary citation

Drory, O.,Frolow, F.,Nelson, N.
Crystal structure of yeast V-ATPase subunit C reveals its stator function
Embo Rep., 5:1148-1152, 2004

PubMed Abstract: 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.

PubMed: 15540116
DOI: 10.1038/sj.embor.7400294

Experimental method

X-RAY DIFFRACTION (1.75 Å)