1ohh

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[[Image:1ohh.gif|left|200px]]<br />
 
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<applet load="1ohh" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ohh, resolution 2.8&Aring;" />
 
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'''BOVINE MITOCHONDRIAL F1-ATPASE COMPLEXED WITH THE INHIBITOR PROTEIN IF1'''<br />
 
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==Overview==
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==BOVINE MITOCHONDRIAL F1-ATPASE complexed with the inhibitor protein IF1==
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In mitochondria, the hydrolytic activity of ATP synthase is prevented by, an inhibitor protein, IF1. The active bovine protein (84 amino acids) is, an alpha-helical dimer with monomers associated via an antiparallel, alpha-helical coiled coil composed of residues 49-81. The N-terminal, inhibitory sequences in the active dimer bind to two F1-ATPases in the, presence of ATP. In the crystal structure of the F1-IF1 complex at 2.8 A, resolution, residues 1-37 of IF1 bind in the alpha(DP)-beta(DP) interface, of F1-ATPase, and also contact the central gamma subunit. The inhibitor, opens the catalytic interface between the alpha(DP) and beta(DP) subunits, relative to previous structures. The presence of ATP in the catalytic site, of the beta(DP) subunit implies that the inhibited state represents a, pre-hydrolysis step on the catalytic pathway of the enzyme.
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<StructureSection load='1ohh' size='340' side='right'caption='[[1ohh]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ohh]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OHH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OHH 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]] 2.8&#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=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=1ohh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ohh OCA], [https://pdbe.org/1ohh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ohh RCSB], [https://www.ebi.ac.uk/pdbsum/1ohh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ohh 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/oh/1ohh_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=1ohh 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 mitochondria, the hydrolytic activity of ATP synthase is prevented by an inhibitor protein, IF1. The active bovine protein (84 amino acids) is an alpha-helical dimer with monomers associated via an antiparallel alpha-helical coiled coil composed of residues 49-81. The N-terminal inhibitory sequences in the active dimer bind to two F1-ATPases in the presence of ATP. In the crystal structure of the F1-IF1 complex at 2.8 A resolution, residues 1-37 of IF1 bind in the alpha(DP)-beta(DP) interface of F1-ATPase, and also contact the central gamma subunit. The inhibitor opens the catalytic interface between the alpha(DP) and beta(DP) subunits relative to previous structures. The presence of ATP in the catalytic site of the beta(DP) subunit implies that the inhibited state represents a pre-hydrolysis step on the catalytic pathway of the enzyme.
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==About this Structure==
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The structure of bovine F1-ATPase in complex with its regulatory protein IF1.,Cabezon E, Montgomery MG, Leslie AG, Walker JE Nat Struct Biol. 2003 Sep;10(9):744-50. Epub 2003 Aug 17. PMID:12923572<ref>PMID:12923572</ref>
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1OHH 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 and ANP 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 Site: PLP. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OHH 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 in complex with its regulatory protein IF1., Cabezon E, Montgomery MG, Leslie AG, Walker JE, Nat Struct Biol. 2003 Sep;10(9):744-50. Epub 2003 Aug 17. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12923572 12923572]
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</div>
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[[Category: Bos taurus]]
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<div class="pdbe-citations 1ohh" 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: Cabezon, E.]]
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[[Category: Leslie, A.G.W.]]
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[[Category: Montgomery, M.G.]]
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[[Category: Walker, J.E.]]
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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 phosphorylase (h+ transporting)]]
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[[Category: atp synthase]]
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[[Category: f1-atpase]]
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[[Category: f1fo atp synthase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 16:54:53 2007''
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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: Cabezon E]]
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[[Category: Leslie AGW]]
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[[Category: Montgomery MG]]
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[[Category: Walker JE]]

Current revision

BOVINE MITOCHONDRIAL F1-ATPASE complexed with the inhibitor protein IF1

PDB ID 1ohh

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