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BOVINE MITOCHONDRIAL F1-ATPASEBOVINE MITOCHONDRIAL F1-ATPASE
Structural highlights
Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedIn 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. Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria.,Abrahams JP, Leslie AG, Lutter R, Walker JE Nature. 1994 Aug 25;370(6491):621-8. PMID:8065448[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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