The structure of bovine F-1-ATPase complexed with the antibiotic inhibitor aurovertin B

van Raaij, M. J. and Abrahams, J. P. and Leslie, A. G. W. and Walker, J. E.. (1996) The structure of bovine F-1-ATPase complexed with the antibiotic inhibitor aurovertin B. Proceedings of the National Academy of Sciences of the United States of America, 93 (14). pp. 6913-6917.

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In the structure of bovine mitochondrial F-1-ATPase that was previously determined with crystals grown in the presence of adenylyl-imidodiphosphate (AMP-PNP) and ADP, the three catalytic beta-subunits have different conformations and nucleotide occupancies. Adenyl-imidodiphosphate is bound to one beta-subunit (beta(TP)), ADP is bound to the second (beta(DP)), and no nucleotide is bound to the third (beta(E)). Here we show that the uncompetitive inhibitor aurovertin B binds to bovine F-1 at two equivalent sites in beta(TP) and beta(E), in a cleft between the nucleotide binding and C-terminal domains. In beta(DP), the aurovertin B pocket is incomplete and is inaccessible to the inhibitor. The aurovertin B bound to beta(TP) interacts with alpha-Glu399 in the adjacent alpha(TP) subunit, whereas the aurovertin B bound to beta(E) is too distant from alpha(E) to make an equivalent interaction. Both sites encompass beta Arg-412, which was shown by mutational studies to be involved in binding aurovertin. Except for minor changes around the aurovertin pockets, the structure of bovine F-1-ATPase is the same as determined previously. Aurovertin B appears to act by preventing closure of the catalytic interfaces, which is essential for a catalytic mechanism involving cyclic interconversion of catalytic sites.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Nano-diffraction of Biological Specimen (Abrahams)
UniBasel Contributors:Abrahams, Jan Pieter
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:National Academy of Sciences
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:05 Nov 2020 14:53
Deposited On:05 Nov 2020 14:53

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