2cly: Difference between revisions

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==Subcomplex of the stator of bovine mitochondrial ATP synthase==
==Subcomplex of the stator of bovine mitochondrial ATP synthase==
<StructureSection load='2cly' size='340' side='right' caption='[[2cly]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
<StructureSection load='2cly' size='340' side='right'caption='[[2cly]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2cly]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CLY FirstGlance]. <br>
<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>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1vzs|1vzs]]</td></tr>
</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>
<tr id='activity'><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 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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cly FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cly OCA], [http://pdbe.org/2cly PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cly RCSB], [http://www.ebi.ac.uk/pdbsum/2cly PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2cly ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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. [[http://www.uniprot.org/uniprot/ATP5J_BOVIN ATP5J_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. Also involved in the restoration of oligomycin-sensitive ATPase activity to depleted F1-F0 complexes. [[http://www.uniprot.org/uniprot/ATP5H_BOVIN ATP5H_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.  
[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</div>
</div>
<div class="pdbe-citations 2cly" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 2cly" style="background-color:#fffaf0;"></div>
==See Also==
*[[ATPase 3D structures|ATPase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bovin]]
[[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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