1efr
From Proteopedia
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|PDB= 1efr |SIZE=350|CAPTION= <scene name='initialview01'>1efr</scene>, resolution 3.1Å | |PDB= 1efr |SIZE=350|CAPTION= <scene name='initialview01'>1efr</scene>, resolution 3.1Å | ||
|SITE= <scene name='pdbsite=CAT:The+Carboxylate+Group+Of+Glutamic+Aci+Residue+Is+Believe+...'>CAT</scene> and <scene name='pdbsite=PLP:The+Residue+Listed+Is+The+LYS+Within+The+P-Loop+(Phospha+...'>PLP</scene> | |SITE= <scene name='pdbsite=CAT:The+Carboxylate+Group+Of+Glutamic+Aci+Residue+Is+Believe+...'>CAT</scene> and <scene name='pdbsite=PLP:The+Residue+Listed+Is+The+LYS+Within+The+P-Loop+(Phospha+...'>PLP</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=AIB:ALPHA-AMINOISOBUTYRIC+ACID'>AIB</scene>, <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=APP:1-ACETYL-2-CARBOXYPIPERIDINE'>APP</scene>, <scene name='pdbligand=BAL:BETA-ALANINE'>BAL</scene>, <scene name='pdbligand=CPI:6-CARBOXYPIPERIDINE'>CPI</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TLX:N1-(2-AMINO-4-METHYLPENTYL)OCTAHYDRO-PYRROLO[1,2-A]+PYRIMIDINE'>TLX</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/ | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1efr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1efr OCA], [http://www.ebi.ac.uk/pdbsum/1efr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1efr RCSB]</span> | ||
}} | }} | ||
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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:[http://www.ncbi.nlm.nih.gov/pubmed/8790345 8790345] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8790345 8790345] | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
| + | [[Category: H(+)-transporting two-sector ATPase]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Transferred entry: 3 6.3 14]] | ||
[[Category: Abrahams, J P.]] | [[Category: Abrahams, J P.]] | ||
[[Category: Buchanan, S K.]] | [[Category: Buchanan, S K.]] | ||
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[[Category: Raaij, M J.Van.]] | [[Category: Raaij, M J.Van.]] | ||
[[Category: Walker, J E.]] | [[Category: Walker, J E.]] | ||
| - | [[Category: ADP]] | ||
| - | [[Category: ANP]] | ||
| - | [[Category: MG]] | ||
[[Category: atp phosphorylase]] | [[Category: atp phosphorylase]] | ||
[[Category: atp synthase]] | [[Category: atp synthase]] | ||
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[[Category: hydrogen ion transport]] | [[Category: hydrogen ion transport]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:01:37 2008'' |
Revision as of 17:01, 30 March 2008
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| , resolution 3.1Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | and | ||||||
| Ligands: | , , , , , , , | ||||||
| Activity: | H(+)-transporting two-sector ATPase, with EC number 3.6.3.14 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 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
1EFR is a Protein complex structure of sequences from Bos taurus. 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 Sun Mar 30 20:01:37 2008
Categories: Bos taurus | H(+)-transporting two-sector ATPase | Protein complex | Abrahams, J P. | Buchanan, S K. | Fearnley, I M. | Leslie, A G.W. | Raaij, M J.Van. | Walker, J E. | Atp phosphorylase | Atp synthase | Complex (ion transport/inhibitor) | F1-atpase | F1f atp synthase | Hydrogen ion transport
