1cow
From Proteopedia
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[[Image:1cow.gif|left|200px]] | [[Image:1cow.gif|left|200px]] | ||
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'''BOVINE MITOCHONDRIAL F1-ATPASE COMPLEXED WITH AUROVERTIN B''' | '''BOVINE MITOCHONDRIAL F1-ATPASE COMPLEXED WITH AUROVERTIN B''' | ||
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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:[http://www.ncbi.nlm.nih.gov/pubmed/8692918 8692918] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8692918 8692918] | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
- | [[Category: H(+)-transporting two-sector ATPase]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Abrahams, J P.]] | [[Category: Abrahams, J P.]] | ||
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[[Category: Raaij, M Van.]] | [[Category: Raaij, M Van.]] | ||
[[Category: Walker, J E.]] | [[Category: Walker, J E.]] | ||
- | [[Category: | + | [[Category: Atp phosphorylase]] |
- | [[Category: | + | [[Category: Atp synthase]] |
- | [[Category: | + | [[Category: F1-atpase]] |
- | [[Category: | + | [[Category: F1f atp synthase]] |
- | [[Category: | + | [[Category: Hydrogen ion transport]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:57:37 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 09:57, 2 May 2008
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. 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 Page seeded by OCA on Fri May 2 12:57:37 2008