An expanded and flexible form of the vacuolar ATPase membrane sector.
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.
Clare
Daniel K
DK
School of Crystallography, Birkbeck College, University of London, Malet Street, London WC1E 7HX, United Kingdom.
Orlova
Elena V
EV
Finbow
Malcolm A
MA
Harrison
Michael A
MA
Findlay
John B C
JB
Saibil
Helen R
HR
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*
D021122:Protein Subunits; D025262:Vacuolar Proton-Translocating ATPases