New insights into one of nature's remarkable catalysts, the ATP synthase.
In the August 10, 2001 issue of Cell, Menz et al. report the crystal structure of a novel inhibited form of the bovine mitochondrial F(1)-ATPase at 2 A resolution, with all three catalytic sites occupied by nucleotide, one of which binds ADP in preference to ATP.
Boyer
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Molecular Biology Institute, University of California, Los Angeles, CA 90095, USA.
D000818:Animals; D001665:Binding Sites; D002384:Catalysis; D002417:Cattle; D018360:Crystallography, X-Ray; D046911:Macromolecular Substances; D008928:Mitochondria / Q000201:enzymology / Q000378:metabolism; D011485:Protein Binding; D020836:Protein Structure, Quaternary; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000378:metabolism
D046911:Macromolecular Substances; D006180:Proton-Translocating ATPases