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2jmx

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[[Image:2jmx.gif|left|200px]]
 
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{{Structure
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==OSCP-NT (1-120) in complex with N-terminal (1-25) alpha subunit from F1-ATPase==
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|PDB= 2jmx |SIZE=350|CAPTION= <scene name='initialview01'>2jmx</scene>
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<StructureSection load='2jmx' size='340' side='right'caption='[[2jmx]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[2jmx]] is a 2 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=2JMX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JMX FirstGlance]. <br>
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|ACTIVITY= [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]
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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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|GENE= ATP5O ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus])
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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=2jmx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jmx OCA], [https://pdbe.org/2jmx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jmx RCSB], [https://www.ebi.ac.uk/pdbsum/2jmx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jmx ProSAT]</span></td></tr>
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}}
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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.
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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/jm/2jmx_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=2jmx 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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The peripheral stalk of ATP synthase acts as a stator holding the alpha(3)beta(3) catalytic subcomplex and the membrane subunit a against the torque of the rotating central stalk and attached c ring. In bovine mitochondria, the N-terminal domain of the oligomycin sensitivity conferral protein (OSCP-NT; residues 1-120) anchors one end of the peripheral stalk to the N-terminal tails of one or more alpha subunits of the F(1) subcomplex. Here, we present an NMR characterisation of the interaction between OSCP-NT and a peptide corresponding to residues 1-25 of the alpha-subunit of bovine F(1)-ATPase. The interaction site contains adjoining hydrophobic surfaces of helices 1 and 5 of OSCP-NT binding to hydrophobic side-chains of the alpha-peptide.
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'''OSCP-NT (1-120) in complex with N-terminal (1-25) alpha subunit from F1-ATPase'''
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How the N-terminal domain of the OSCP subunit of bovine F1Fo-ATP synthase interacts with the N-terminal region of an alpha subunit.,Carbajo RJ, Kellas FA, Yang JC, Runswick MJ, Montgomery MG, Walker JE, Neuhaus D J Mol Biol. 2007 Apr 27;368(2):310-8. Epub 2007 Feb 22. PMID:17355883<ref>PMID:17355883</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 2jmx" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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The peripheral stalk of ATP synthase acts as a stator holding the alpha(3)beta(3) catalytic subcomplex and the membrane subunit a against the torque of the rotating central stalk and attached c ring. In bovine mitochondria, the N-terminal domain of the oligomycin sensitivity conferral protein (OSCP-NT; residues 1-120) anchors one end of the peripheral stalk to the N-terminal tails of one or more alpha subunits of the F(1) subcomplex. Here, we present an NMR characterisation of the interaction between OSCP-NT and a peptide corresponding to residues 1-25 of the alpha-subunit of bovine F(1)-ATPase. The interaction site contains adjoining hydrophobic surfaces of helices 1 and 5 of OSCP-NT binding to hydrophobic side-chains of the alpha-peptide.
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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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2JMX 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=2JMX OCA].
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__TOC__
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</StructureSection>
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==Reference==
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How the N-terminal domain of the OSCP subunit of bovine F1Fo-ATP synthase interacts with the N-terminal region of an alpha subunit., Carbajo RJ, Kellas FA, Yang JC, Runswick MJ, Montgomery MG, Walker JE, Neuhaus D, J Mol Biol. 2007 Apr 27;368(2):310-8. Epub 2007 Feb 22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17355883 17355883]
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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: Carbajo RJ]]
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[[Category: Carbajo, R J.]]
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[[Category: Kellas FA]]
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[[Category: Kellas, F A.]]
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[[Category: Montgomery MG]]
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[[Category: Montgomery, M G.]]
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[[Category: Neuhaus D]]
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[[Category: Neuhaus, D.]]
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[[Category: Runswick MJ]]
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[[Category: Runswick, M J.]]
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[[Category: Walker JE]]
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[[Category: Walker, J E.]]
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[[Category: Yang J]]
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[[Category: Yang, J.]]
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[[Category: oscp-nt alpha-nt complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:42:59 2008''
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Current revision

OSCP-NT (1-120) in complex with N-terminal (1-25) alpha subunit from F1-ATPase

PDB ID 2jmx

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