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2bo5

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==BOVINE OLIGOMYCIN SENSITIVITY CONFERRAL PROTEIN N-TERMINAL DOMAIN==
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<StructureSection load='2bo5' size='340' side='right' caption='[[2bo5]], [[NMR_Ensembles_of_Models | 44 NMR models]]' scene=''>
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==Bovine oligomycin sensitivity conferral protein N-terminal domain==
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<StructureSection load='2bo5' size='340' side='right'caption='[[2bo5]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2bo5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BO5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BO5 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2bo5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BO5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BO5 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bo5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bo5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bo5 RCSB], [http://www.ebi.ac.uk/pdbsum/2bo5 PDBsum]</span></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=2bo5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bo5 OCA], [https://pdbe.org/2bo5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bo5 RCSB], [https://www.ebi.ac.uk/pdbsum/2bo5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bo5 ProSAT]</span></td></tr>
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<table>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ATPO_BOVIN ATPO_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. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bo/2bo5_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bo/2bo5_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</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/chain_selection.php?pdb_ID=2ata ConSurf].
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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=2bo5 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 2bo5" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Carbajo, R J.]]
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[[Category: Large Structures]]
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[[Category: Kellas, F A.]]
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[[Category: Carbajo RJ]]
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[[Category: Montgomery, M G.]]
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[[Category: Kellas FA]]
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[[Category: Neuhaus, D.]]
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[[Category: Montgomery MG]]
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[[Category: Runswick, M J.]]
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[[Category: Neuhaus D]]
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[[Category: Walker, J E.]]
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[[Category: Runswick MJ]]
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[[Category: Alpha-subunit]]
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[[Category: Walker JE]]
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[[Category: Atp synthase]]
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[[Category: Beta-subunit]]
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[[Category: Binding interface]]
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[[Category: Chemical shift mapping]]
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[[Category: Chemical shift perturbation]]
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[[Category: Hydrogen ion transport]]
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[[Category: Hydrolase]]
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[[Category: Ion transport]]
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[[Category: Mitochondrion]]
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[[Category: Oscp]]
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[[Category: Peripheral stalk]]
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[[Category: Protein-protein interaction]]
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[[Category: Titration]]
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[[Category: Transit peptide]]
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[[Category: Transport]]
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Current revision

Bovine oligomycin sensitivity conferral protein N-terminal domain

PDB ID 2bo5

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