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[[Image:2wss.png|left|200px]]
==THE STRUCTURE OF THE MEMBRANE EXTRINSIC REGION OF BOVINE ATP SYNTHASE==
<StructureSection load='2wss' size='340' side='right' caption='[[2wss]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2wss]] is a 25 chain structure with sequence 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=2WSS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WSS FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br>
<tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2v7q|2v7q]], [[2jiz|2jiz]], [[1bmf|1bmf]], [[1nbm|1nbm]], [[2w6e|2w6e]], [[2w6f|2w6f]], [[2jj1|2jj1]], [[2w6g|2w6g]], [[1e1q|1e1q]], [[1w0j|1w0j]], [[2w6i|2w6i]], [[1cow|1cow]], [[1h8h|1h8h]], [[1e1r|1e1r]], [[1ohh|1ohh]], [[1qo1|1qo1]], [[1vzs|1vzs]], [[2cly|2cly]], [[2jdi|2jdi]], [[1efr|1efr]], [[1h8e|1h8e]], [[2jj2|2jj2]], [[2bo5|2bo5]], [[1e79|1e79]], [[2ck3|2ck3]], [[2w6j|2w6j]], [[2w6h|2w6h]], [[1w0k|1w0k]]</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>
<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=2wss FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wss OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2wss RCSB], [http://www.ebi.ac.uk/pdbsum/2wss PDBsum]</span></td></tr>
<table>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ws/2wss_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The structure of the complex between bovine mitochondrial F(1)-ATPase and a stator subcomplex has been determined at a resolution of 3.2 A. The resolved region of the stator contains residues 122-207 of subunit b; residues 5-25 and 35-57 of F(6); 3 segments of subunit d from residues 30-40, 65-74, and 85-91; and residues 1-146 and 169-189 of the oligomycin sensitivity conferral protein (OSCP). The stator subcomplex represents its membrane distal part, and its structure has been augmented with an earlier structure of a subcomplex containing residues 79-183, 3-123, and 5-70 of subunits b, d, and F(6), respectively, which extends to the surface of the inner membrane of the mitochondrion. The N-terminal domain of the OSCP links the stator with F(1)-ATPase via alpha-helical interactions with the N-terminal region of subunit alpha(E). Its C-terminal domain makes extensive helix-helix interactions with the C- terminal alpha-helix of subunit b from residues 190-207. Subunit b extends as a continuous 160-A long alpha-helix from residue 188 back to residue 79 near to the surface of the inner mitochondrial membrane. This helix appears to be stiffened by other alpha-helices in subunits d and F(6), but the structure can bend inward toward the F(1) domain around residue 146 of subunit b. The linker region between the 2 domains of the OSCP also appears to be flexible, enabling the stator to adjust its shape as it passes over the changing profile of the F(1) domain during a catalytic cycle. The structure of the membrane extrinsic part of bovine ATP synthase is now complete.


{{STRUCTURE_2wss|  PDB=2wss  |  SCENE=  }}
The structure of the membrane extrinsic region of bovine ATP synthase.,Rees DM, Leslie AG, Walker JE Proc Natl Acad Sci U S A. 2009 Dec 7. PMID:19995987<ref>PMID:19995987</ref>


===THE STRUCTURE OF THE MEMBRANE EXTRINSIC REGION OF BOVINE ATP SYNTHASE===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_19995987}}
 
==About this Structure==
[[2wss]] is a 25 chain structure with sequence 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=2WSS OCA].


==See Also==
==See Also==
*[[ATP synthase|ATP synthase]]
*[[ATPase|ATPase]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:019995987</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Leslie, A G.W.]]
[[Category: Leslie, A G.W.]]