An expanded and flexible form of the vacuolar ATPase membrane sector

Structure. 2006 Jul;14(7):1149-56. doi: 10.1016/j.str.2006.05.014.

Abstract

The vacuolar ATPase integral membrane c-ring from Nephrops norvegicus occurs in paired complexes in a double membrane. Using cryo-electron microscopy and single particle image processing of 2D crystals, we have obtained a projection structure of the c-ring of N. norvegicus. The c-ring was found to be very flexible, most likely as a result of an expanded conformation of the c subunits. This structure may support a role for the vacuolar ATPase c-rings in membrane fusion.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cell Membrane / enzymology
  • Cryoelectron Microscopy
  • Crystallography
  • Molecular Sequence Data
  • Nephropidae / enzymology*
  • Protein Conformation
  • Protein Subunits / chemistry
  • Vacuolar Proton-Translocating ATPases / chemistry*
  • Vacuolar Proton-Translocating ATPases / ultrastructure*

Substances

  • Protein Subunits
  • Vacuolar Proton-Translocating ATPases