1efr

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[[Image:1efr.jpg|left|200px]]<br /><applet load="1efr" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1efr, resolution 3.1&Aring;" />
 
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'''BOVINE MITOCHONDRIAL F1-ATPASE COMPLEXED WITH THE PEPTIDE ANTIBIOTIC EFRAPEPTIN'''<br />
 
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==Overview==
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==BOVINE MITOCHONDRIAL F1-ATPASE COMPLEXED WITH THE PEPTIDE ANTIBIOTIC EFRAPEPTIN==
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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.
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<StructureSection load='1efr' size='340' side='right'caption='[[1efr]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1efr]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Tolypocladium_inflatum Tolypocladium inflatum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EFR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EFR FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <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=BAL:BETA-ALANINE'>BAL</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>, <scene name='pdbligand=YCP:(2S)-PIPERIDINE-2-CARBOXYLIC+ACID'>YCP</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1efr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1efr OCA], [https://pdbe.org/1efr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1efr RCSB], [https://www.ebi.ac.uk/pdbsum/1efr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1efr ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ATPA_BOVIN ATPA_BOVIN] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ef/1efr_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1efr ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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:8790345<ref>PMID:8790345</ref>
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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 <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=ANP:'>ANP</scene> and <scene name='pdbligand=ADP:'>ADP</scene> 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] Known structural/functional Sites: <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>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EFR OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=8790345 8790345]
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</div>
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[[Category: Bos taurus]]
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<div class="pdbe-citations 1efr" style="background-color:#fffaf0;"></div>
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[[Category: Protein complex]]
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[[Category: Transferred entry: 3.6.3.14]]
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[[Category: Abrahams, J.P.]]
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[[Category: Buchanan, S.K.]]
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[[Category: Fearnley, I.M.]]
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[[Category: Leslie, A.G.W.]]
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[[Category: Raaij, M.J.Van.]]
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[[Category: Walker, J.E.]]
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[[Category: ADP]]
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[[Category: ANP]]
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[[Category: MG]]
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[[Category: atp phosphorylase]]
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[[Category: atp synthase]]
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[[Category: complex (ion transport/inhibitor)]]
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[[Category: f1-atpase]]
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[[Category: f1f atp synthase]]
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[[Category: hydrogen ion transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:39:08 2008''
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==See Also==
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*[[ATPase 3D structures|ATPase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Bos taurus]]
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[[Category: Large Structures]]
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[[Category: Tolypocladium inflatum]]
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[[Category: Abrahams JP]]
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[[Category: Buchanan SK]]
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[[Category: Fearnley IM]]
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[[Category: Leslie AGW]]
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[[Category: Van Raaij MJ]]
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[[Category: Walker JE]]

Current revision

BOVINE MITOCHONDRIAL F1-ATPASE COMPLEXED WITH THE PEPTIDE ANTIBIOTIC EFRAPEPTIN

PDB ID 1efr

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