6za9: Difference between revisions
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==== | ==Fo domain of Ovine ATP synthase== | ||
<StructureSection load='6za9' size='340' side='right'caption='[[6za9]]' scene=''> | <StructureSection load='6za9' size='340' side='right'caption='[[6za9]], [[Resolution|resolution]] 3.76Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6za9]] is a 17 chain structure with sequence from [https://en.wikipedia.org/wiki/Ovis_aries Ovis aries]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZA9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZA9 FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.76Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CDL:CARDIOLIPIN'>CDL</scene>, <scene name='pdbligand=LHG:1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE'>LHG</scene>, <scene name='pdbligand=S12:O-[(S)-HYDROXY{[(2S)-2-HYDROXY-3-(OCTADEC-9-ENOYLOXY)PROPYL]OXY}PHOSPHORYL]-L-SERINE'>S12</scene></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=6za9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6za9 OCA], [https://pdbe.org/6za9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6za9 RCSB], [https://www.ebi.ac.uk/pdbsum/6za9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6za9 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Disease == | |||
[https://www.uniprot.org/uniprot/AT5G1_SHEEP AT5G1_SHEEP] This protein is the major protein stored in the storage bodies of animals or humans affected with ceroid lipofuscinosis (Batten disease). | |||
== Function == | |||
[https://www.uniprot.org/uniprot/AT5G1_SHEEP AT5G1_SHEEP] 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. A homomeric c-ring of probably 10 subunits is part of the complex rotary element. | |||
==See Also== | |||
*[[ATPase 3D structures|ATPase 3D structures]] | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Ovis aries]] | ||
[[Category: Pinke G]] | |||
[[Category: Sazanov LA]] | |||
[[Category: Zhou L]] | |||
Latest revision as of 10:40, 1 May 2024
Fo domain of Ovine ATP synthaseFo domain of Ovine ATP synthase
Structural highlights
DiseaseAT5G1_SHEEP This protein is the major protein stored in the storage bodies of animals or humans affected with ceroid lipofuscinosis (Batten disease). FunctionAT5G1_SHEEP 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. A homomeric c-ring of probably 10 subunits is part of the complex rotary element. See Also |
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