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

Autor(en): Svergun, DI
Konrad, S
Huss, M 
Koch, MHJ
Wieczorek, H 
Altendorf, K 
Volkov, VV
Gruber, G
Stichwörter: Biochemistry & Molecular Biology; DIRECT SHAPE DETERMINATION; KDA SUBUNIT; MEMBRANE; NEUROSPORA-CRASSA; PURIFICATION; SMALL-ANGLE-SCATTERING; SYNCHROTRON RADIATION; TOBACCO HORNWORM MIDGUT; V-ATPASE; VACUOLAR H+-ATPASE
Erscheinungsdatum: 1998
Herausgeber: AMER CHEMICAL SOC
Journal: BIOCHEMISTRY
Volumen: 37
Ausgabe: 51
Startseite: 17659
Seitenende: 17663
Zusammenfassung: 
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 ab 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 seventh mass with a length of about 11.0 nm extends perpendicularly to the center of the hexameric unit. This central mass is presumed to be the stalk that 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 subunits. The features of the V-1 and F-1 ATPase reveal structural homologies and diversities of the key components of the complexes.
ISSN: 00062960
DOI: 10.1021/bi982367a

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