1U7L

Crystal structure of yeast V-ATPase subunit C reveals its stator function

(2004) EMBO Rep 5: 1148-1152

• PubMed: 15540116 Search on PubMedSearch on PubMed Central
• DOI: https://doi.org/10.1038/sj.embor.7400294
• Primary Citation of Related Structures:  
  1U7L


• 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.

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Organizational Affiliation: 

Department of Biochemistry, The George S Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel.