Elucidation of the stator organization in the V-ATPase of Neurospora crassa

J Mol Biol. 2005 Jun 10;349(3):659-69. doi: 10.1016/j.jmb.2005.04.033.


V-ATPases are membrane protein complexes that pump protons in the lumen of various subcellular compartments at the expense of ATP. Proton pumping is done by a rotary mechanism that requires a static connection between the membrane pumping domain (V(0)) and the extrinsic catalytic head (V(1)). This static connection is composed of several known subunits of the V-ATPase, but their location and topological relationships are still a matter of controversy. Here, we propose a model for the V-ATPase of Neurospora crassa on the basis of single-particle analysis by electron microscopy. Comparison of the resulting map to that of the A-ATPase from Thermus thermophilus allows the positioning of two subunits in the static connecting region that are unique to eukaryotic V-ATPases (C and H). These two subunits seem to be located on opposite sides of a semicircular arrangement of the peripheral connecting elements, suggesting a role in stabilizing the stator in V-ATPases.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Intracellular Membranes / enzymology
  • Microscopy, Electron
  • Models, Molecular
  • Neurospora crassa / enzymology*
  • Protein Structure, Tertiary
  • Vacuolar Proton-Translocating ATPases / chemistry*
  • Vacuolar Proton-Translocating ATPases / isolation & purification
  • Vacuoles / enzymology


  • Vacuolar Proton-Translocating ATPases