Crystallography Centre Department of Pharmacology,
University of Western Australia and Western Australian Institute for Medical
Research, Nedlands Western Australia 6907,
Australia.
ATP synthases (F1Fo-ATPases) use energy released
by the movement of protons down a transmembrane electrochemical gradient to
drive the synthesis of ATP, the universal biological energy currency. Proton
flow through Fo drives rotation of a ring of c-subunits and a complex
of the and -subunits, causing cyclical conformational changes
in F1 that are required for catalysis. The crystal structure of
a large portion of F1 has been resolved. However, the structure
of the central portion of the enzyme, through which conformational changes
in Fo are communicated to F1, has until now remained
elusive. Here we report the crystal structure of a complex of the -subunit
and the central domain of the -subunit refined at 2.1 Å resolution.
The structure reveals how rotation of these subunits causes large conformational
changes in F1, and thereby provides new insights into energy coupling
between Fo and F1.
−
complex of ATP synthase
and 
-subunits, causing cyclical conformational changes
in F1 that are required for catalysis. The crystal structure of
a large portion of F1 has been resolved. However, the structure
of the central portion of the enzyme, through which conformational changes
in Fo are communicated to F1, has until now remained
elusive. Here we report the crystal structure of a complex of the 
