Novel features in the structure of bovine ATP synthase.
The F1F0-ATP synthase from bovine heart mitochondria catalyses the synthesis of ATP from ADP and inorganic phosphate by using the energy of an electrochemical proton gradient derived from electron transport. The enzyme consists of three major domains: the globular F1catalytic domain of known atomic structure lies outside the lipid bilayer and is attached by a central stalk to the intrinsic membrane domain, F0, which transports protons through the membrane. Proton transport through F0evokes structural changes that are probably transmitted by rotation of the stalk to the catalytic sites in F1. In an alpha3beta3gamma1subcomplex, the rotation of the central gamma subunit driven by ATP hydrolysis has been visualised by optical microscopy. In order to prevent the alpha3beta3structure from following the rotation of the central gamma subunit, it has been proposed that the enzyme might have a stator connecting static parts in F0to alpha3beta3,thereby keeping it fixed relative to the rotating parts. Here we present electron microscopy images that reveal three new features in bovine F1F0-ATPase, one of which could be a stator. The second feature is a collar structure above the membrane domain and the third feature is some additional density on top of the F1domain.
Karrasch
S
S
Laboratory of Molecular Biology, MRC, Hills Road, Cambridge, CB2 2QH, United Kingdom. karrsch@ruf.uni-freiburg.de
Walker
J E
JE
D000818:Animals; D002417:Cattle; D008854:Microscopy, Electron; D008929:Mitochondria, Heart / Q000201:enzymology; D015999:Multivariate Analysis; D011487:Protein Conformation; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000648:ultrastructure*; D012399:Rotation; D012995:Solubility
D006180:Proton-Translocating ATPases