6t15

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==The III2-IV(5B)1 respiratory supercomplex from S. cerevisiae==
==The III2-IV(5B)1 respiratory supercomplex from S. cerevisiae==
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<StructureSection load='6t15' size='340' side='right'caption='[[6t15]]' scene=''>
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<StructureSection load='6t15' size='340' side='right'caption='[[6t15]], [[Resolution|resolution]] 3.29&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T15 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6T15 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6t15]] is a 33 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast], [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T15 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6T15 FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6t15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t15 OCA], [http://pdbe.org/6t15 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6t15 RCSB], [http://www.ebi.ac.uk/pdbsum/6t15 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6t15 ProSAT]</span></td></tr>
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</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=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=CUA:DINUCLEAR+COPPER+ION'>CUA</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</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=PCF:1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE'>PCF</scene>, <scene name='pdbligand=PEF:DI-PALMITOYL-3-SN-PHOSPHATIDYLETHANOLAMINE'>PEF</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">COX13, YGL191W, G1341 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Quinol--cytochrome-c_reductase Quinol--cytochrome-c reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=7.1.1.8 7.1.1.8] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6t15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t15 OCA], [http://pdbe.org/6t15 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6t15 RCSB], [http://www.ebi.ac.uk/pdbsum/6t15 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6t15 ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/COX1_YEAST COX1_YEAST]] Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. [[http://www.uniprot.org/uniprot/COX13_YEAST COX13_YEAST]] Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Not necessary for assembly of the enzyme complex but interacts with ATP and thereby modulates the enzyme activity. [[http://www.uniprot.org/uniprot/QCR7_YEAST QCR7_YEAST]] Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain that generates an electrochemical potential coupled to ATP synthesis. The complex couples electron transfer from ubiquinol to cytochrome c. QCR7 is involved in redox-linked proton pumping. [[http://www.uniprot.org/uniprot/QCR2_YEAST QCR2_YEAST]] Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain that generates an electrochemical potential coupled to ATP synthesis. The complex couples electron transfer from ubiquinol to cytochrome c. QCR2 is required for the assembly of the complex. [[http://www.uniprot.org/uniprot/QCR1_YEAST QCR1_YEAST]] Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain that generates an electrochemical potential coupled to ATP synthesis. The complex couples electron transfer from ubiquinol to cytochrome c. COR1 may mediate formation of the complex between cytochromes c and c1. [[http://www.uniprot.org/uniprot/RCF2_YEAST RCF2_YEAST]] Assembly factor that plays a role in the assembly of the respiratory chain supercomplexes (SCs) composed of ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV). May be required for late-stage assembly of the COX12 and COX13 subunits (PubMed:22342701, PubMed:22310663). Required for the generation and maintenance of a normal proton motive force (PMF) across the inner mitochondrial membrane (IMM) by preventing proton leakage through an inactive population of CIV that accumulates when RCF1 and/or RCF2 proteins are absent (PubMed:30683696, PubMed:31591265).<ref>PMID:22310663</ref> <ref>PMID:22342701</ref> <ref>PMID:30683696</ref> <ref>PMID:31591265</ref> [[http://www.uniprot.org/uniprot/COX6_YEAST COX6_YEAST]] This is the heme A-containing chain of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. [[http://www.uniprot.org/uniprot/COX3_YEAST COX3_YEAST]] Subunits I, II and III form the functional core of the enzyme complex. [[http://www.uniprot.org/uniprot/QCR6_YEAST QCR6_YEAST]] Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain that generates an electrochemical potential coupled to ATP synthesis. The complex couples electron transfer from ubiquinol to cytochrome c. QCR6 may mediate formation of the complex between cytochromes c and c1. [[http://www.uniprot.org/uniprot/CYB_YEAST CYB_YEAST]] Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain that generates an electrochemical potential coupled to ATP synthesis. The complex couples electron transfer from ubiquinol to cytochrome c. [[http://www.uniprot.org/uniprot/QCR9_YEAST QCR9_YEAST]] Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain that generates an electrochemical potential coupled to ATP synthesis. The complex couples electron transfer from ubiquinol to cytochrome c. QCR9 is required for formation of a fully functional complex. [[http://www.uniprot.org/uniprot/COX2_YEAST COX2_YEAST]] Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. Subunit 2 transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit 1. [[http://www.uniprot.org/uniprot/COX12_YEAST COX12_YEAST]] This protein is one of the nuclear-coded polypeptide chains of cytochrome c oxidase, the terminal oxidase in mitochondrial electron transport. This protein may be one of the heme-binding subunits of the oxidase. [[http://www.uniprot.org/uniprot/COX5B_YEAST COX5B_YEAST]] Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of COX2 and heme A of COX1 to the active site in COX1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.[UniProtKB:P00424] [[http://www.uniprot.org/uniprot/QCR8_YEAST QCR8_YEAST]] Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain that generates an electrochemical potential coupled to ATP synthesis. The complex couples electron transfer from ubiquinol to cytochrome c. QCR8, together with cytochrome b, binds to ubiquinone. [[http://www.uniprot.org/uniprot/CY1_YEAST CY1_YEAST]] Heme-containing component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain that generates an electrochemical potential coupled to ATP synthesis. The complex couples electron transfer from ubiquinol to cytochrome c. [[http://www.uniprot.org/uniprot/COX9_YEAST COX9_YEAST]] This small integral protein plays a role in holoenzyme assembly or stability. [[http://www.uniprot.org/uniprot/QCR10_YEAST QCR10_YEAST]] Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain that generates an electrochemical potential coupled to ATP synthesis. The complex couples electron transfer from ubiquinol to cytochrome c. QCR10 is required for stable association of the iron-sulfur protein with the complex. [[http://www.uniprot.org/uniprot/UCRI_YEAST UCRI_YEAST]] Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. The complex couples electron transfer from ubiquinol to cytochrome c.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The organization of the mitochondrial electron transport chain proteins into supercomplexes (SCs) is now undisputed; however, their assembly process, or the role of differential expression isoforms, remain to be determined. In Saccharomyces cerevisiae, cytochrome c oxidase (CIV) forms SCs of varying stoichiometry with cytochrome bc 1 (CIII). Recent studies have revealed, in normoxic growth conditions, an interface made exclusively by Cox5A, the only yeast respiratory protein that exists as one of two isoforms depending on oxygen levels. Here we present the cryo-EM structures of the III2-IV1 and III2-IV2 SCs containing the hypoxic isoform Cox5B solved at 3.4 and 2.8 A, respectively. We show that the change of isoform does not affect SC formation or activity, and that SC stoichiometry is dictated by the level of CIII/CIV biosynthesis. Comparison of the CIV(5B)- and CIV(5A)-containing SC structures highlighted few differences, found mainly in the region of Cox5. Additional density was revealed in all SCs, independent of the CIV isoform, in a pocket formed by Cox1, Cox3, Cox12, and Cox13, away from the CIII-CIV interface. In the CIV(5B)-containing hypoxic SCs, this could be confidently assigned to the hypoxia-induced gene 1 (Hig1) type 2 protein Rcf2. With conserved residues in mammalian Hig1 proteins and Cox3/Cox12/Cox13 orthologs, we propose that Hig1 type 2 proteins are stoichiometric subunits of CIV, at least when within a III-IV SC.
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Rcf2 revealed in cryo-EM structures of hypoxic isoforms of mature mitochondrial III-IV supercomplexes.,Hartley AM, Meunier B, Pinotsis N, Marechal A Proc Natl Acad Sci U S A. 2020 Apr 14. pii: 1920612117. doi:, 10.1073/pnas.1920612117. PMID:32291341<ref>PMID:32291341</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6t15" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Baker's yeast]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Hartley A]]
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[[Category: Quinol--cytochrome-c reductase]]
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[[Category: Marechal A]]
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[[Category: Saccharomyces cerevisiae s288c]]
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[[Category: Pinotsis N]]
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[[Category: Hartley, A]]
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[[Category: Marechal, A]]
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[[Category: Pinotsis, N]]
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[[Category: Cytochrome c oxidase cytochrome bc1 mitochondria respiratory chain supercomplex]]
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[[Category: Electron transport]]
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[[Category: Oxidoreductase]]
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[[Category: Oxidoreductase-electron transport complex]]

Revision as of 06:33, 6 May 2020

The III2-IV(5B)1 respiratory supercomplex from S. cerevisiae

PDB ID 6t15

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