Quaternary structure of V-1 and F-1 ATPase: Significance of structural homologies and diversities

The V-1 ATPase from the tobacco hornworm Manduca sexta and the Escherichia coli F-1 ATPase were characterized by small-angle X-ray scattering (SAXS). The radii of gyration (R-g) of the complexes were 6.2 +/- 0.1 and 4.7 +/- 0 .02 nm, respectively. The shape of the M. sexta V-1 ATPase was determined a b initio from the scattering data showing six masses, presumed to be the A and B subunits, arranged in an alternating manner about a 3-fold axis. A se venth mass with a length of about 11.0 nm extends perpendicularly to the ce nter of the hexameric unit. This central mass is presumed to be the stalk t hat connects V-1 with the membrane domain (V-o) in the intact V1Vo-ATPase. In comparison, the shape of the F-1 ATPase from E. coli possesses a quasi-3 -fold symmetry over the major part of the enzyme. The overall asymmetry of the structure is given by a stem, assumed to include the central stalk subu nits. The features of the V-1 and F-1 ATPase reveal structural homologies a nd diversities of the key components of the complexes.