1cow
From Proteopedia
| Line 4: | Line 4: | ||
==Overview== | ==Overview== | ||
| - | In the structure of bovine mitochondrial F1-ATPase that was previously | + | 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== | ==About this Structure== | ||
| Line 13: | Line 13: | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Transferred entry: 3 | + | [[Category: Transferred entry: 3 6.3 14]] |
| - | [[Category: Abrahams, J | + | [[Category: Abrahams, J P.]] |
| - | [[Category: Leslie, A | + | [[Category: Leslie, A G.W.]] |
| - | [[Category: Raaij, M | + | [[Category: Raaij, M Van.]] |
| - | [[Category: Walker, J | + | [[Category: Walker, J E.]] |
[[Category: ADP]] | [[Category: ADP]] | ||
[[Category: ANP]] | [[Category: ANP]] | ||
| Line 28: | Line 28: | ||
[[Category: hydrogen ion transport]] | [[Category: hydrogen ion transport]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:08:11 2008'' |
Revision as of 10:08, 21 February 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 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
Page seeded by OCA on Thu Feb 21 12:08:11 2008
