2cly: Difference between revisions

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[[Image:2cly.png|left|200px]]


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==Subcomplex of the stator of bovine mitochondrial ATP synthase==
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<StructureSection load='2cly' size='340' side='right'caption='[[2cly]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2cly]] is a 6 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=2CLY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CLY 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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2cly FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cly OCA], [https://pdbe.org/2cly PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cly RCSB], [https://www.ebi.ac.uk/pdbsum/2cly PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cly ProSAT]</span></td></tr>
{{STRUCTURE_2cly|  PDB=2cly  |  SCENE= }}
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== Function ==
[https://www.uniprot.org/uniprot/AT5F1_BOVIN AT5F1_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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
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    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cl/2cly_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/main_output.php?pdb_ID=2cly ConSurf].
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== Publication Abstract from PubMed ==
The structure of most of the peripheral stalk, or stator, of the F-ATPase from bovine mitochondria, determined at 2.8 A resolution, contains residues 79-183, 3-123 and 5-70 of subunits b, d and F6, respectively. It consists of a continuous curved alpha-helix about 160 A long in the single b-subunit, augmented by the predominantly alpha-helical d- and F6-subunits. The structure occupies most of the peripheral stalk in a low-resolution structure of the F-ATPase. The long helix in subunit b extends from near to the top of the F1 domain to the surface of the membrane domain, and it probably continues unbroken across the membrane. Its uppermost region interacts with the oligomycin sensitivity conferral protein, bound to the N-terminal region of one alpha-subunit in the F1 domain. Various features suggest that the peripheral stalk is probably rigid rather than resembling a flexible rope. It remains unclear whether the transient storage of energy required by the rotary mechanism takes place in the central stalk or in the peripheral stalk or in both domains.


===SUBCOMPLEX OF THE STATOR OF BOVINE MITOCHONDRIAL ATP SYNTHASE===
On the structure of the stator of the mitochondrial ATP synthase.,Dickson VK, Silvester JA, Fearnley IM, Leslie AG, Walker JE EMBO J. 2006 Jun 21;25(12):2911-8. Epub 2006 Jun 8. PMID:16791136<ref>PMID:16791136</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_16791136}}, adds the Publication Abstract to the page
*[[ATPase 3D structures|ATPase 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 16791136 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_16791136}}
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</StructureSection>
==About this Structure==
[[2cly]] is a 6 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=2CLY OCA].
 
==Reference==
<ref group="xtra">PMID:16791136</ref><ref group="xtra">PMID:16754973</ref><references group="xtra"/>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Dickson, V Kane.]]
[[Category: Large Structures]]
[[Category: Fearnley, I M.]]
[[Category: Fearnley IM]]
[[Category: Leslie, A G.W.]]
[[Category: Kane Dickson V]]
[[Category: Silvester, J A.]]
[[Category: Leslie AGW]]
[[Category: Walker, J E.]]
[[Category: Silvester JA]]
[[Category: Acetylation]]
[[Category: Walker JE]]
[[Category: Atp synthase]]
[[Category: Hydrogen ion transport]]
[[Category: Hydrolase]]
[[Category: Ion transport]]
[[Category: Mitochondria]]
[[Category: Mitochondrion]]
[[Category: Peripheral stalk]]
[[Category: Stator]]
[[Category: Transit peptide]]
[[Category: Transport]]

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