7o3e: Difference between revisions
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==== | ==Murine supercomplex CIII2CIV in the intermediate locked conformation== | ||
<StructureSection load='7o3e' size='340' side='right'caption='[[7o3e]]' scene=''> | <StructureSection load='7o3e' size='340' side='right'caption='[[7o3e]], [[Resolution|resolution]] 3.60Å' 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 [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | <table><tr><td colspan='2'>[[7o3e]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7O3E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7O3E FirstGlance]. <br> | ||
</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=7o3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7o3e OCA], [https://pdbe.org/7o3e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7o3e RCSB], [https://www.ebi.ac.uk/pdbsum/7o3e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7o3e ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.6Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3PE:1,2-DIACYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE'>3PE</scene>, <scene name='pdbligand=CDL:CARDIOLIPIN'>CDL</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=CUA:DINUCLEAR+COPPER+ION'>CUA</scene>, <scene name='pdbligand=HEA:HEME-A'>HEA</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PC1:1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE'>PC1</scene>, <scene name='pdbligand=TGL:TRISTEAROYLGLYCEROL'>TGL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=7o3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7o3e OCA], [https://pdbe.org/7o3e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7o3e RCSB], [https://www.ebi.ac.uk/pdbsum/7o3e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7o3e ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The enzymes of the mitochondrial electron transport chain are key players of cell metabolism. Despite being active when isolated, in vivo they associate into supercomplexes(1), whose precise role is debated. Supercomplexes CIII(2)CIV(1-2) (refs. (2,3)), CICIII(2) (ref. (4)) and CICIII(2)CIV (respirasome)(5-10) exist in mammals, but in contrast to CICIII(2) and the respirasome, to date the only known eukaryotic structures of CIII(2)CIV(1-2) come from Saccharomyces cerevisiae(11,12) and plants(13), which have different organization. Here we present the first, to our knowledge, structures of mammalian (mouse and ovine) CIII(2)CIV and its assembly intermediates, in different conformations. We describe the assembly of CIII(2)CIV from the CIII(2) precursor to the final CIII(2)CIV conformation, driven by the insertion of the N terminus of the assembly factor SCAF1 (ref. (14)) deep into CIII(2), while its C terminus is integrated into CIV. Our structures (which include CICIII(2) and the respirasome) also confirm that SCAF1 is exclusively required for the assembly of CIII(2)CIV and has no role in the assembly of the respirasome. We show that CIII(2) is asymmetric due to the presence of only one copy of subunit 9, which straddles both monomers and prevents the attachment of a second copy of SCAF1 to CIII(2), explaining the presence of one copy of CIV in CIII(2)CIV in mammals. Finally, we show that CIII(2) and CIV gain catalytic advantage when assembled into the supercomplex and propose a role for CIII(2)CIV in fine tuning the efficiency of electron transfer in the electron transport chain. | |||
Structure and assembly of the mammalian mitochondrial supercomplex CIII(2)CIV.,Vercellino I, Sazanov LA Nature. 2021 Oct;598(7880):364-367. doi: 10.1038/s41586-021-03927-z. Epub 2021 , Oct 6. PMID:34616041<ref>PMID:34616041</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7o3e" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Cytochrome bc1 3D structures|Cytochrome bc1 3D structures]] | |||
*[[Cytochrome c oxidase 3D structures|Cytochrome c oxidase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mus musculus]] | ||
[[Category: Sazanov LA]] | |||
[[Category: Vercellino I]] | |||
Latest revision as of 12:01, 17 October 2024
Murine supercomplex CIII2CIV in the intermediate locked conformationMurine supercomplex CIII2CIV in the intermediate locked conformation
Structural highlights
Publication Abstract from PubMedThe enzymes of the mitochondrial electron transport chain are key players of cell metabolism. Despite being active when isolated, in vivo they associate into supercomplexes(1), whose precise role is debated. Supercomplexes CIII(2)CIV(1-2) (refs. (2,3)), CICIII(2) (ref. (4)) and CICIII(2)CIV (respirasome)(5-10) exist in mammals, but in contrast to CICIII(2) and the respirasome, to date the only known eukaryotic structures of CIII(2)CIV(1-2) come from Saccharomyces cerevisiae(11,12) and plants(13), which have different organization. Here we present the first, to our knowledge, structures of mammalian (mouse and ovine) CIII(2)CIV and its assembly intermediates, in different conformations. We describe the assembly of CIII(2)CIV from the CIII(2) precursor to the final CIII(2)CIV conformation, driven by the insertion of the N terminus of the assembly factor SCAF1 (ref. (14)) deep into CIII(2), while its C terminus is integrated into CIV. Our structures (which include CICIII(2) and the respirasome) also confirm that SCAF1 is exclusively required for the assembly of CIII(2)CIV and has no role in the assembly of the respirasome. We show that CIII(2) is asymmetric due to the presence of only one copy of subunit 9, which straddles both monomers and prevents the attachment of a second copy of SCAF1 to CIII(2), explaining the presence of one copy of CIV in CIII(2)CIV in mammals. Finally, we show that CIII(2) and CIV gain catalytic advantage when assembled into the supercomplex and propose a role for CIII(2)CIV in fine tuning the efficiency of electron transfer in the electron transport chain. Structure and assembly of the mammalian mitochondrial supercomplex CIII(2)CIV.,Vercellino I, Sazanov LA Nature. 2021 Oct;598(7880):364-367. doi: 10.1038/s41586-021-03927-z. Epub 2021 , Oct 6. PMID:34616041[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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