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1efr
From Proteopedia
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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 [Transferred entry: 3.6.3.14], with EC number [3.6.1.34]. Structure known Active Sites: CAT and PLP. 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 Tue Oct 30 15:10:31 2007
Categories: Bos taurus | Protein complex | Transferred entry: 3.6.3.14 | Abrahams, J.P. | Buchanan, S.K. | Fearnley, I.M. | Leslie, A.G.W. | Raaij, M.J.Van. | Walker, J.E. | ADP | ANP | MG | Atp phosphorylase | Atp synthase | Complex (ion transport/inhibitor) | F1-atpase | F1f atp synthase | Hydrogen ion transport
