Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria.
In the crystal structure of bovine mitochondrial F1-ATPase determined at 2.8 A resolution, the three catalytic beta-subunits differ in conformation and in the bound nucleotide. The structure supports a catalytic mechanism in intact ATP synthase in which the three catalytic subunits are in different states of the catalytic cycle at any instant. Interconversion of the states may be achieved by rotation of the alpha 3 beta 3 subassembly relative to an alpha-helical domain of the gamma-subunit.
Abrahams
J P
JP
Medical Research Council Laboratory of Molecular Biology, Cambridge, UK.
Leslie
A G
AG
Lutter
R
R
Walker
J E
JE
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002384:Catalysis; D002417:Cattle; D003196:Computer Graphics; D018360:Crystallography, X-Ray; D008929:Mitochondria, Heart / Q000201:enzymology*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009711:Nucleotides / Q000378:metabolism; D011487:Protein Conformation; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000378:metabolism
D009711:Nucleotides; D006180:Proton-Translocating ATPases