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= | + | |LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=AUR:AUROVERTIN+B'>AUR</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/ | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cow FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cow OCA], [http://www.ebi.ac.uk/pdbsum/1cow PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cow RCSB]</span> | ||
}} | }} | ||
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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: Transferred entry: 3 6.3 14]] | ||
[[Category: Abrahams, J P.]] | [[Category: Abrahams, J P.]] | ||
[[Category: Leslie, A G.W.]] | [[Category: Leslie, A G.W.]] | ||
[[Category: Raaij, M Van.]] | [[Category: Raaij, M Van.]] | ||
[[Category: Walker, J E.]] | [[Category: Walker, J E.]] | ||
| - | [[Category: ADP]] | ||
| - | [[Category: ANP]] | ||
| - | [[Category: AUR]] | ||
| - | [[Category: MG]] | ||
[[Category: atp phosphorylase]] | [[Category: atp phosphorylase]] | ||
[[Category: atp synthase]] | [[Category: atp synthase]] | ||
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[[Category: hydrogen ion transport]] | [[Category: hydrogen ion transport]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:25:42 2008'' |
Revision as of 16:25, 30 March 2008
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| , resolution 3.1Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | and | ||||||
| Ligands: | , , , | ||||||
| Activity: | H(+)-transporting two-sector ATPase, with EC number 3.6.3.14 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
Page seeded by OCA on Sun Mar 30 19:25:42 2008
