1cow
From Proteopedia
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|PDB= 1cow |SIZE=350|CAPTION= <scene name='initialview01'>1cow</scene>, resolution 3.1Å | |PDB= 1cow |SIZE=350|CAPTION= <scene name='initialview01'>1cow</scene>, resolution 3.1Å | ||
|SITE= <scene name='pdbsite=CAT:The+Carboxylate+Group+Of+GLU+Residue+Is+Believed+To+Acti+...'>CAT</scene> and <scene name='pdbsite=PLP:The+Residue+Listed+Is+The+LYS+Within+The+P-Loop+(Phospha+...'>PLP</scene> | |SITE= <scene name='pdbsite=CAT:The+Carboxylate+Group+Of+GLU+Residue+Is+Believed+To+Acti+...'>CAT</scene> and <scene name='pdbsite=PLP:The+Residue+Listed+Is+The+LYS+Within+The+P-Loop+(Phospha+...'>PLP</scene> | ||
| - | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=ADP:ADENOSINE-5 | + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene> and <scene name='pdbligand=AUR:AUROVERTIN B'>AUR</scene> |
|ACTIVITY= [http://en.wikipedia.org/wiki/Transferred_entry:_3.6.3.14 Transferred entry: 3.6.3.14], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.34 3.6.1.34] | |ACTIVITY= [http://en.wikipedia.org/wiki/Transferred_entry:_3.6.3.14 Transferred entry: 3.6.3.14], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.34 3.6.1.34] | ||
|GENE= | |GENE= | ||
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[[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 Sun Mar 23 11:24:18 2008'' |
Revision as of 09:24, 23 March 2008
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| , resolution 3.1Å | |||||||
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| Sites: | and | ||||||
| Ligands: | , , and | ||||||
| Activity: | Transferred entry: 3.6.3.14, with EC number 3.6.1.34 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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