title: An expanded and flexible form of the vacuolar ATPase membrane sector.
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.
authors.affiliation: School of Crystallography, Birkbeck College, University of London, Malet Street, London WC1E 7HX, United Kingdom.
authors.forename: Daniel K
authors.initials: DK
authors.lastname: Clare
authors.forename: Elena V
authors.initials: EV
authors.lastname: Orlova
authors.forename: Malcolm A
authors.initials: MA
authors.lastname: Finbow
authors.forename: Michael A
authors.initials: MA
authors.lastname: Harrison
authors.forename: John B C
authors.initials: JB
authors.lastname: Findlay
authors.forename: Helen R
authors.initials: HR
authors.lastname: Saibil
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002462:Cell Membrane / Q000201:enzymology; D020285:Cryoelectron Microscopy; D003461:Crystallography; D008969:Molecular Sequence Data; D008121:Nephropidae / Q000201:enzymology*; D011487:Protein Conformation; D021122:Protein Subunits / Q000737:chemistry; D025262:Vacuolar Proton-Translocating ATPases / Q000737:chemistry* / Q000648:ultrastructure*
chemical_list: D021122:Protein Subunits; D025262:Vacuolar Proton-Translocating ATPases