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| | {{STRUCTURE_1e1q| PDB=1e1q | SCENE= }} | | {{STRUCTURE_1e1q| PDB=1e1q | SCENE= }} |
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| - | '''BOVINE MITOCHONDRIAL F1-ATPASE AT 100K'''
| + | ===BOVINE MITOCHONDRIAL F1-ATPASE AT 100K=== |
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| - | ==Overview==
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| - | BACKGROUND: The globular domain of the membrane-associated F(1)F(o)-ATP synthase complex can be detached intact as a water-soluble fragment known as F(1)-ATPase. It consists of five different subunits, alpha, beta, gamma, delta and epsilon, assembled with the stoichiometry 3:3:1:1:1. In the crystal structure of bovine F(1)-ATPase determined previously at 2.8 A resolution, the three catalytic beta subunits and the three noncatalytic alpha subunits are arranged alternately around a central alpha-helical coiled coil in the gamma subunit. In the crystals, the catalytic sites have different nucleotide occupancies. One contains the triphosphate form of the nucleotide, the second contains the diphosphate, and the third is unoccupied. Fluoroaluminate complexes have been shown to mimic the transition state in several ATP and GTP hydrolases. In order to understand more about its catalytic mechanism, F(1)-ATPase was inhibited with Mg(2+)ADP and aluminium fluoride and the structure of the inhibited complex was determined by X-ray crystallography. RESULTS: The structure of bovine F(1)-ATPase inhibited with Mg(2+)ADP and aluminium fluoride determined at 2.5 A resolution differs little from the original structure with bound AMP-PNP and ADP. The nucleotide occupancies of the alpha and beta subunits are unchanged except that both aluminium trifluoride and Mg(2+)ADP are bound in the nucleotide-binding site of the beta(DP) subunit. The presence of aluminium fluoride is accompanied by only minor adjustments in the surrounding protein. CONCLUSIONS: The structure appears to mimic a possible transition state. The coordination of the aluminofluoride group has many features in common with other aluminofluoride-NTP hydrolase complexes. Apparently, once nucleotide is bound to the catalytic beta subunit, no additional major structural changes are required for catalysis to occur.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_10873854}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10873854 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_10873854}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: F1-atpase]] | | [[Category: F1-atpase]] |
| | [[Category: F1fo atp synthase]] | | [[Category: F1fo atp synthase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:32:56 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:59:55 2008'' |
Revision as of 21:00, 30 June 2008
Template:STRUCTURE 1e1q
BOVINE MITOCHONDRIAL F1-ATPASE AT 100K
Template:ABSTRACT PUBMED 10873854
About this Structure
1E1Q is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.
Reference
Structure of bovine mitochondrial F(1)-ATPase inhibited by Mg(2+) ADP and aluminium fluoride., Braig K, Menz RI, Montgomery MG, Leslie AG, Walker JE, Structure. 2000 Jun 15;8(6):567-73. PMID:10873854
Page seeded by OCA on Mon Jun 30 23:59:55 2008
