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Quaternary structure of V1 and F1 ATPase: significance of structural homologies and diversities

Authors :
Svergun, Dmitri I.
Konrad, Stephanie
Huss, Markus
Koch, Michel H.J.
Wieczorek, Helmut
Altendorf, Karlheinz
Volkov, Vladimir V.
Gruber, Gerhard
Source :
Biochemistry. Dec 22, 1998, Vol. 37 Issue 51, p17659, 5 p.
Publication Year :
1998

Abstract

The quaternary structure of the V1 ATPase from the tobacco hornworm Manduca sexta and the F1 ATPase from Escherichia coli was characterized using small-angle X-ray scattering. The radii of gyration of the V1 and F1 complexes as well as the shape of the V1 ATPase were also determined. Experimental results showed that a seventh mass, which is thought to be the stalk that links V1 with the membrane domain V0 in the intact V1V0-ATPase, extends perpendicularly to the center of the hexameric unit.

Details

ISSN :
00062960
Volume :
37
Issue :
51
Database :
Gale General OneFile
Journal :
Biochemistry
Publication Type :
Academic Journal
Accession number :
edsgcl.53688190