1ohh
From Proteopedia
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| - | [[Image:1ohh.jpg|left|200px]] | + | [[Image:1ohh.jpg|left|200px]] |
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| - | '''BOVINE MITOCHONDRIAL F1-ATPASE COMPLEXED WITH THE INHIBITOR PROTEIN IF1''' | + | {{Structure |
| + | |PDB= 1ohh |SIZE=350|CAPTION= <scene name='initialview01'>1ohh</scene>, resolution 2.8Å | ||
| + | |SITE= <scene name='pdbsite=PLP:Mg+Binding+Site+For+Chain+F'>PLP</scene> | ||
| + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER'>ANP</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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''BOVINE MITOCHONDRIAL F1-ATPASE COMPLEXED WITH THE INHIBITOR PROTEIN IF1''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1OHH is a [ | + | 1OHH is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OHH OCA]. |
==Reference== | ==Reference== | ||
| - | The structure of bovine F1-ATPase in complex with its regulatory protein IF1., Cabezon E, Montgomery MG, Leslie AG, Walker JE, Nat Struct Biol. 2003 Sep;10(9):744-50. Epub 2003 Aug 17. PMID:[http:// | + | The structure of bovine F1-ATPase in complex with its regulatory protein IF1., Cabezon E, Montgomery MG, Leslie AG, Walker JE, Nat Struct Biol. 2003 Sep;10(9):744-50. Epub 2003 Aug 17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12923572 12923572] |
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: f1fo atp synthase]] | [[Category: f1fo atp synthase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:10:58 2008'' |
Revision as of 11:10, 20 March 2008
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| , resolution 2.8Å | |||||||
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| Sites: | |||||||
| 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 THE INHIBITOR PROTEIN IF1
Overview
In mitochondria, the hydrolytic activity of ATP synthase is prevented by an inhibitor protein, IF1. The active bovine protein (84 amino acids) is an alpha-helical dimer with monomers associated via an antiparallel alpha-helical coiled coil composed of residues 49-81. The N-terminal inhibitory sequences in the active dimer bind to two F1-ATPases in the presence of ATP. In the crystal structure of the F1-IF1 complex at 2.8 A resolution, residues 1-37 of IF1 bind in the alpha(DP)-beta(DP) interface of F1-ATPase, and also contact the central gamma subunit. The inhibitor opens the catalytic interface between the alpha(DP) and beta(DP) subunits relative to previous structures. The presence of ATP in the catalytic site of the beta(DP) subunit implies that the inhibited state represents a pre-hydrolysis step on the catalytic pathway of the enzyme.
About this Structure
1OHH is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.
Reference
The structure of bovine F1-ATPase in complex with its regulatory protein IF1., Cabezon E, Montgomery MG, Leslie AG, Walker JE, Nat Struct Biol. 2003 Sep;10(9):744-50. Epub 2003 Aug 17. PMID:12923572
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