Crystal structure of yeast V-ATPase subunit C reveals its stator function.
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.
Drory
Omri
O
Department of Biochemistry, The George S Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel.
Frolow
Felix
F
Nelson
Nathan
N
D000199:Actins / Q000378:metabolism; D003460:Crystallization; D003461:Crystallography; D019143:Evolution, Molecular; D018260:Gelsolin / Q000378:metabolism; D006801:Humans; D008854:Microscopy, Electron; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000502:physiology; D025262:Vacuolar Proton-Translocating ATPases / Q000737:chemistry* / Q000502:physiology
D000199:Actins; D018260:Gelsolin; D029701:Saccharomyces cerevisiae Proteins; C447616:VMA5 protein, S cerevisiae; D025262:Vacuolar Proton-Translocating ATPases