1ohh

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[[Image:1ohh.jpg|left|200px]]
 
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{{Structure
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==BOVINE MITOCHONDRIAL F1-ATPASE complexed with the inhibitor protein IF1==
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|PDB= 1ohh |SIZE=350|CAPTION= <scene name='initialview01'>1ohh</scene>, resolution 2.8&Aring;
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<StructureSection load='1ohh' size='340' side='right'caption='[[1ohh]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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|SITE= <scene name='pdbsite=PLP:Mg+Binding+Site+For+Chain+F'>PLP</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
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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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|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>
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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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|GENE=
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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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|DOMAIN=
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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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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ohh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ohh OCA], [http://www.ebi.ac.uk/pdbsum/1ohh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ohh RCSB]</span>
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== Function ==
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}}
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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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'''BOVINE MITOCHONDRIAL F1-ATPASE COMPLEXED WITH THE INHIBITOR PROTEIN IF1'''
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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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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1ohh" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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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*[[ATPase 3D structures|ATPase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1OHH is a [[Protein complex]] structure of sequences from [http://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].
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__TOC__
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</StructureSection>
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==Reference==
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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://www.ncbi.nlm.nih.gov/pubmed/12923572 12923572]
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: H(+)-transporting two-sector ATPase]]
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[[Category: Large Structures]]
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[[Category: Protein complex]]
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[[Category: Cabezon E]]
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[[Category: Cabezon, E.]]
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[[Category: Leslie AGW]]
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[[Category: Leslie, A G.W.]]
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[[Category: Montgomery MG]]
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[[Category: Montgomery, M G.]]
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[[Category: Walker JE]]
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[[Category: Walker, J E.]]
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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://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:45:24 2008''
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Current revision

BOVINE MITOCHONDRIAL F1-ATPASE complexed with the inhibitor protein IF1

PDB ID 1ohh

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