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| | ==Structure of a functional obligate respiratory supercomplex from Mycobacterium smegmatis== | | ==Structure of a functional obligate respiratory supercomplex from Mycobacterium smegmatis== |
| - | <StructureSection load='6hwh' size='340' side='right' caption='[[6hwh]], [[Resolution|resolution]] 3.30Å' scene=''> | + | <SX load='6hwh' size='340' side='right' viewer='molstar' caption='[[6hwh]], [[Resolution|resolution]] 3.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6hwh]] is a 28 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycs2 Mycs2] and [http://en.wikipedia.org/wiki/Mycobacterium_smegmatis_mc2_155 Mycobacterium smegmatis mc2 155]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HWH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HWH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6hwh]] is a 22 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_smegmatis_MC2_155 Mycolicibacterium smegmatis MC2 155]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HWH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6HWH FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CDL:CARDIOLIPIN'>CDL</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HAS:HEME-AS'>HAS</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MQ9:MENAQUINONE-9'>MQ9</scene></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]] 3.3Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></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=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MQ9:MENAQUINONE-9'>MQ9</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">qcrB, MSMEI_4163 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=246196 MYCS2])</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=6hwh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hwh OCA], [https://pdbe.org/6hwh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6hwh RCSB], [https://www.ebi.ac.uk/pdbsum/6hwh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6hwh ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquinol--cytochrome-c_reductase Ubiquinol--cytochrome-c reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.10.2.2 1.10.2.2] </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=6hwh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hwh OCA], [http://pdbe.org/6hwh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hwh RCSB], [http://www.ebi.ac.uk/pdbsum/6hwh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hwh ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/A0R056_MYCS2 A0R056_MYCS2]] Part of cytochrome c oxidase, its function is unknown.[PIRNR:PIRNR017385] [[http://www.uniprot.org/uniprot/A0R0M4_MYCS2 A0R0M4_MYCS2]] 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.[RuleBase:RU363061] | + | [https://www.uniprot.org/uniprot/A0R051_MYCS2 A0R051_MYCS2] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6hwh" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6hwh" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Cytochrome c oxidase 3D structures|Cytochrome c oxidase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| - | </StructureSection> | + | </SX> |
| - | [[Category: Mycobacterium smegmatis mc2 155]] | + | [[Category: Large Structures]] |
| - | [[Category: Mycs2]] | + | [[Category: Mycolicibacterium smegmatis MC2 155]] |
| - | [[Category: Ubiquinol--cytochrome-c reductase]]
| + | [[Category: Adelroth P]] |
| - | [[Category: Adelroth, P]] | + | [[Category: Benlekbir S]] |
| - | [[Category: Benlekbir, S]] | + | [[Category: Brzezinski P]] |
| - | [[Category: Brzezinski, P]] | + | [[Category: Fedotovskaya O]] |
| - | [[Category: Fedotovskaya, O]] | + | [[Category: Guo H]] |
| - | [[Category: Guo, H]] | + | [[Category: Hogbom M]] |
| - | [[Category: Hogbom, M]] | + | [[Category: Kuang Q]] |
| - | [[Category: Kuang, Q]] | + | [[Category: Nitharwal RG]] |
| - | [[Category: Nitharwal, R G]] | + | [[Category: Rubinstein JL]] |
| - | [[Category: Rubinstein, J L]] | + | [[Category: Schafer J]] |
| - | [[Category: Schafer, J]] | + | [[Category: Sjostrand D]] |
| - | [[Category: Sjostrand, D]] | + | [[Category: Wiseman B]] |
| - | [[Category: Wiseman, B]] | + | |
| - | [[Category: Cryo-em]]
| + | |
| - | [[Category: Electron transport]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Mycobacterium]]
| + | |
| - | [[Category: Respiratory supercomplex]]
| + | |
| Structural highlights
Function
A0R051_MYCS2
Publication Abstract from PubMed
In the mycobacterial electron-transport chain, respiratory complex III passes electrons from menaquinol to complex IV, which in turn reduces oxygen, the terminal acceptor. Electron transfer is coupled to transmembrane proton translocation, thus establishing the electrochemical proton gradient that drives ATP synthesis. We isolated, biochemically characterized, and determined the structure of the obligate III2IV2 supercomplex from Mycobacterium smegmatis, a model for Mycobacterium tuberculosis. The supercomplex has quinol:O2 oxidoreductase activity without exogenous cytochrome c and includes a superoxide dismutase subunit that may detoxify reactive oxygen species produced during respiration. We found menaquinone bound in both the Qo and Qi sites of complex III. The complex III-intrinsic diheme cytochrome cc subunit, which functionally replaces both cytochrome c1 and soluble cytochrome c in canonical electron-transport chains, displays two conformations: one in which it provides a direct electronic link to complex IV and another in which it serves as an electrical switch interrupting the connection.
Structure of a functional obligate complex III2IV2 respiratory supercomplex from Mycobacterium smegmatis.,Wiseman B, Nitharwal RG, Fedotovskaya O, Schafer J, Guo H, Kuang Q, Benlekbir S, Sjostrand D, Adelroth P, Rubinstein JL, Brzezinski P, Hogbom M Nat Struct Mol Biol. 2018 Dec;25(12):1128-1136. doi: 10.1038/s41594-018-0160-3., Epub 2018 Dec 5. PMID:30518849[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Wiseman B, Nitharwal RG, Fedotovskaya O, Schafer J, Guo H, Kuang Q, Benlekbir S, Sjostrand D, Adelroth P, Rubinstein JL, Brzezinski P, Hogbom M. Structure of a functional obligate complex III2IV2 respiratory supercomplex from Mycobacterium smegmatis. Nat Struct Mol Biol. 2018 Dec;25(12):1128-1136. doi: 10.1038/s41594-018-0160-3., Epub 2018 Dec 5. PMID:30518849 doi:http://dx.doi.org/10.1038/s41594-018-0160-3
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