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Title
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Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria.
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Authors
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J.P.Abrahams,
A.G.Leslie,
R.Lutter,
J.E.Walker.
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Ref.
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Nature, 1994,
370,
621-628.
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PubMed id
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Abstract
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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.
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