1efr
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /> <applet load="1efr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1efr, resolution 3.1Å" /> '''BOVINE MITOCHONDRIAL...)
Next diff →
Revision as of 17:32, 29 October 2007
|
BOVINE MITOCHONDRIAL F1-ATPASE COMPLEXED WITH THE PEPTIDE ANTIBIOTIC EFRAPEPTIN
Overview
In the previously determined structure of mitochondrial F1-ATPase, 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., AMP-PNP and ADP are bound to subunits beta TP and beta DP, respectively, and the third beta-subunit (beta E) has no bound nucleotide. The, efrapeptins are a closely related family of modified linear peptides, containing 15 amino acids that inhibit both ATP synthesis and hydrolysis, by binding to the F1 catalytic domain of F1F0-ATP synthase. In crystals of, F1-ATPase grown in the presence of both nucleotides and inhibitor, efrapeptin is bound to a unique site in the central cavity of the enzyme., Its binding is associated with small ... [(full description)]
About this Structure
1EFR is a [Protein complex] structure of sequences from [Bos taurus] with MG, ANP and ADP as [ligands]. Active as [[1]], with EC number [3.6.1.34]. Full crystallographic information is available from [OCA].
Reference
The structure of bovine F1-ATPase complexed with the peptide antibiotic efrapeptin., Abrahams JP, Buchanan SK, Van Raaij MJ, Fearnley IM, Leslie AG, Walker JE, Proc Natl Acad Sci U S A. 1996 Sep 3;93(18):9420-4. PMID:8790345
Page seeded by OCA on Mon Oct 29 19:36:51 2007
