1cow
From Proteopedia
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BOVINE MITOCHONDRIAL F1-ATPASE COMPLEXED WITH AUROVERTIN B
Overview
In the structure of bovine mitochondrial F1-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., Adenylyl-imidodiphosphate is bound to one beta-subunit (betaTP), ADP is, bound to the second (betaDP), and no nucleotide is bound to the third, (betaE). Here we show that the uncompetitive inhibitor aurovertin B binds, to bovine F1 at two equivalent sites in betaTP and betaE, in a cleft, between the nucleotide binding and C-terminal domains. In betaDP, the, aurovertin B pocket is incomplete and is inaccessible to the inhibitor., The aurovertin B bound to betaTP interacts with alpha-Glu399 in the, adjacent alphaTP subunit, whereas the aurovertin B bound to betaE is too, distant from alphaE to make an equivalent interaction. Both sites, encompass betaArg-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 F1-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.
About this Structure
1COW is a Protein complex structure of sequences from Bos taurus with , , and as ligands. Active as Transferred entry: 3.6.3.14, with EC number 3.6.1.34 Known structural/functional Sites: and . Full crystallographic information is available from OCA.
Reference
The structure of bovine F1-ATPase complexed with the antibiotic inhibitor aurovertin B., van Raaij MJ, Abrahams JP, Leslie AG, Walker JE, Proc Natl Acad Sci U S A. 1996 Jul 9;93(14):6913-7. PMID:8692918
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