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==Overview== | ==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 ... | 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 structural changes in side chains of, F1-ATPase around the binding pocket. Efrapeptin makes hydrophobic contacts, with the alpha-helical structure in the gamma-subunit, which traverses the, cavity, and with subunit beta E and the two adjacent alpha-subunits. Two, intermolecular hydrogen bonds could also form. Intramolecular hydrogen, bonds probably help to stabilize efrapeptin's two domains (residues 1-6, and 9-15, respectively), which are connected by a flexible region (beta, Ala-7 and Gly-8). Efrapeptin appears to inhibit F1-ATPase by blocking the, conversion of subunit beta E to a nucleotide binding conformation, as, would be required by an enzyme mechanism involving cyclic interconversion, of catalytic sites. | ||
==About this Structure== | ==About this Structure== | ||
1EFR is a | 1EFR is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with MG, ANP and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Structure known Active Sites: CAT and PLP. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EFR OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: hydrogen ion transport]] | [[Category: hydrogen ion transport]] | ||
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Revision as of 15:04, 5 November 2007
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BOVINE MITOCHONDRIAL F1-ATPASE COMPLEXED WITH THE PEPTIDE ANTIBIOTIC EFRAPEPTIN
OverviewOverview
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 structural changes in side chains of, F1-ATPase around the binding pocket. Efrapeptin makes hydrophobic contacts, with the alpha-helical structure in the gamma-subunit, which traverses the, cavity, and with subunit beta E and the two adjacent alpha-subunits. Two, intermolecular hydrogen bonds could also form. Intramolecular hydrogen, bonds probably help to stabilize efrapeptin's two domains (residues 1-6, and 9-15, respectively), which are connected by a flexible region (beta, Ala-7 and Gly-8). Efrapeptin appears to inhibit F1-ATPase by blocking the, conversion of subunit beta E to a nucleotide binding conformation, as, would be required by an enzyme mechanism involving cyclic interconversion, of catalytic sites.
About this StructureAbout 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.
ReferenceReference
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
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