1COW

BOVINE MITOCHONDRIAL F1-ATPASE COMPLEXED WITH AUROVERTIN B

Summary for 1COW

• Entry DOI: 10.2210/pdb1cow/pdb
• Descriptor: BOVINE MITOCHONDRIAL F1-ATPASE, MAGNESIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (8 entities in total)
• Functional Keywords: atp phosphorylase, hydrogen ion transport, atp synthase, f1f atp synthase, f1-atpase
• Biological source: Bos taurus (cattle); More
• Total number of polymer chains: 7
• Total formula weight: 354860.30

Authors

van Raaij, M.J.,Abrahams, J.P.,Leslie, A.G.W.,Walker, J.E. (deposition date: 1996-05-08, release date: 1996-08-17, Last modification date: 2024-02-07)

Primary citation

van Raaij, M.J.,Abrahams, J.P.,Leslie, A.G.,Walker, J.E.
The structure of bovine F1-ATPase complexed with the antibiotic inhibitor aurovertin B.
Proc.Natl.Acad.Sci.USA, 93:6913-6917, 1996

PubMed Abstract: 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.

PubMed: 8692918
DOI: 10.1073/pnas.93.14.6913

Experimental method

X-RAY DIFFRACTION (3.1 Å)