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| | '''Unreleased structure''' |
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| ==III2-IV1 respiratory supercomplex from S. pombe==
| | The entry 8q1b is ON HOLD until Paper Publication |
| <StructureSection load='8q1b' size='340' side='right'caption='[[8q1b]], [[Resolution|resolution]] 3.40Å' scene=''>
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| == Structural highlights ==
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| <table><tr><td colspan='2'>[[8q1b]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8Q1B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8Q1B 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">Electron Microscopy, [[Resolution|Resolution]] 3.4Å</td></tr>
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| <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=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=U10:UBIQUINONE-10'>U10</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=8q1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8q1b OCA], [https://pdbe.org/8q1b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8q1b RCSB], [https://www.ebi.ac.uk/pdbsum/8q1b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8q1b ProSAT]</span></td></tr>
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| </table>
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| == Function ==
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| [https://www.uniprot.org/uniprot/MPPB_SCHPO MPPB_SCHPO] Catalytic subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins (By similarity). Preferentially, cleaves after an arginine at position P2 (By similarity).[UniProtKB:P10507][UniProtKB:Q03346]
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| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| The respiratory chain in aerobic organisms is composed of a number of membrane-bound protein complexes that link electron transfer to proton translocation across the membrane. In mitochondria, the final electron acceptor, complex IV (CIV), receives electrons from dimeric complex III (CIII(2)), via a mobile electron carrier, cytochrome c. In the present study, we isolated the CIII(2)CIV supercomplex from the fission yeast Schizosaccharomyces pombe and determined its structure with bound cyt. c using single-particle electron cryomicroscopy. A respiratory supercomplex factor 2 was found to be bound at CIV distally positioned in the supercomplex. In addition to the redox-active metal sites, we found a metal ion, presumably Zn(2+), coordinated in the CIII subunit Cor1, which is encoded by the same gene (qcr1) as the mitochondrial-processing peptidase subunit beta. Our data show that the isolated CIII(2)CIV supercomplex displays proteolytic activity suggesting a dual role of CIII(2) in S. pombe. As in the supercomplex from S. cerevisiae, subunit Cox5 of CIV faces towards one CIII monomer, but in S. pombe, the two complexes are rotated relative to each other by ~45 degrees . This orientation yields equal distances between the cyt. c binding sites at CIV and at each of the two CIII monomers. The structure shows cyt. c bound at four positions, but only along one of the two symmetrical branches. Overall, this combined structural and functional study reveals the integration of peptidase activity with the CIII(2) respiratory system and indicates a two-dimensional cyt. c diffusion mechanism within the CIII(2)-CIV supercomplex.
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| Structure and function of the S. pombe III-IV-cyt c supercomplex.,Moe A, Dimogkioka AR, Rapaport D, Ojemyr LN, Brzezinski P Proc Natl Acad Sci U S A. 2023 Nov 14;120(46):e2307697120. doi: , 10.1073/pnas.2307697120. Epub 2023 Nov 8. PMID:37939086<ref>PMID:37939086</ref>
| | Authors: Moe, A., Brzezinski, P. |
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| | Description: III2-IV1 respiratory supercomplex from S. pombe |
| </div>
| | [[Category: Unreleased Structures]] |
| <div class="pdbe-citations 8q1b" style="background-color:#fffaf0;"></div>
| | [[Category: Brzezinski, P]] |
| == References ==
| | [[Category: Moe, A]] |
| <references/>
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| __TOC__
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| </StructureSection>
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| [[Category: Large Structures]] | |
| [[Category: Schizosaccharomyces pombe]]
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| [[Category: Brzezinski P]] | |
| [[Category: Moe A]] | |
Unreleased structure
The entry 8q1b is ON HOLD until Paper Publication
Authors: Moe, A., Brzezinski, P.
Description: III2-IV1 respiratory supercomplex from S. pombe