Document Detail

Ground state structure of F1-ATPase from bovine heart mitochondria at 1.9 A resolution.
MedLine Citation:
PMID:  17350959     Owner:  NLM     Status:  MEDLINE    
The structure of bovine F(1)-ATPase, crystallized in the presence of AMP-PNP and ADP, but in the absence of azide, has been determined at 1.9A resolution. This structure has been compared with the previously described structure of bovine F(1)-ATPase determined at 1.95A resolution with crystals grown under the same conditions but in the presence of azide. The two structures are extremely similar, but they differ in the nucleotides that are bound to the catalytic site in the beta(DP)-subunit. In the present structure, the nucleotide binding sites in the beta(DP)- and beta(TP)-subunits are both occupied by AMP-PNP, whereas in the earlier structure, the beta(TP) site was occupied by AMP-PNP and the beta(DP) site by ADP, where its binding is enhanced by a bound azide ion. Also, the conformation of the side chain of the catalytically important residue, alphaArg-373 differs in the beta(DP)- and beta(TP)-subunits. Thus, the structure with bound azide represents the ADP inhibited state of the enzyme, and the new structure represents a ground state intermediate in the active catalytic cycle of ATP hydrolysis.
Matthew W Bowler; Martin G Montgomery; Andrew G W Leslie; John E Walker
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Publication Detail:
Type:  Journal Article     Date:  2007-03-09
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  282     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2007 May 
Date Detail:
Created Date:  2007-05-07     Completed Date:  2007-06-28     Revised Date:  2014-02-19    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  14238-42     Citation Subset:  IM    
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MeSH Terms
Adenosine Diphosphate / metabolism
Adenylyl Imidodiphosphate / metabolism
Binding Sites
Catalytic Domain
Crystallography, X-Ray
Mitochondria, Heart / enzymology*
Models, Molecular
Protein Conformation*
Proton-Translocating ATPases / chemistry*,  metabolism
Grant Support
MC_U105184325//Medical Research Council; MC_U105663150//Medical Research Council
Reg. No./Substance:
0/Azides; 25612-73-1/Adenylyl Imidodiphosphate; 61D2G4IYVH/Adenosine Diphosphate; EC ATPases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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