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| | <StructureSection load='5xmj' size='340' side='right'caption='[[5xmj]], [[Resolution|resolution]] 3.60Å' scene=''> | | <StructureSection load='5xmj' size='340' side='right'caption='[[5xmj]], [[Resolution|resolution]] 3.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5xmj]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_gigas Desulfovibrio gigas] and [http://en.wikipedia.org/wiki/Desulfovibrio_gigas_dsm_1382_=_atcc_19364 Desulfovibrio gigas dsm 1382 = atcc 19364]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XMJ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5XMJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5xmj]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Megalodesulfovibrio_gigas Megalodesulfovibrio gigas] and [https://en.wikipedia.org/wiki/Megalodesulfovibrio_gigas_DSM_1382_=_ATCC_19364 Megalodesulfovibrio gigas DSM 1382 = ATCC 19364]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XMJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XMJ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=FUM:FUMARIC+ACID'>FUM</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=MQ7:MENAQUINONE-7'>MQ7</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.6Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Succinate_dehydrogenase_(quinone) Succinate dehydrogenase (quinone)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.5.1 1.3.5.1] </span></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=FUM:FUMARIC+ACID'>FUM</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=MQ7:MENAQUINONE-7'>MQ7</scene></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=5xmj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xmj OCA], [http://pdbe.org/5xmj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xmj RCSB], [http://www.ebi.ac.uk/pdbsum/5xmj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xmj ProSAT]</span></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=5xmj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xmj OCA], [https://pdbe.org/5xmj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xmj RCSB], [https://www.ebi.ac.uk/pdbsum/5xmj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xmj ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/T2GB49_MEGG1 T2GB49_MEGG1] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Desulfovibrio gigas]] | |
| - | [[Category: Desulfovibrio gigas dsm 1382 = atcc 19364]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chen, C J]] | + | [[Category: Megalodesulfovibrio gigas]] |
| - | [[Category: Guan, H H]] | + | [[Category: Megalodesulfovibrio gigas DSM 1382 = ATCC 19364]] |
| - | [[Category: Hsieh, Y C]] | + | [[Category: Chen CJ]] |
| - | [[Category: Lin, P R]] | + | [[Category: Guan HH]] |
| - | [[Category: Electron transfer]] | + | [[Category: Hsieh YC]] |
| - | [[Category: Electron transport]] | + | [[Category: Lin PR]] |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Proton transfer]]
| + | |
| - | [[Category: Qfr]]
| + | |
| Structural highlights
5xmj is a 12 chain structure with sequence from Megalodesulfovibrio gigas and Megalodesulfovibrio gigas DSM 1382 = ATCC 19364. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 3.6Å |
| Ligands: | , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
T2GB49_MEGG1
Publication Abstract from PubMed
The membrane-embedded quinol:fumarate reductase (QFR) in anaerobic bacteria catalyzes the reduction of fumarate to succinate by quinol in the anaerobic respiratory chain. The electron/proton-transfer pathways in QFRs remain controversial. Here we report the crystal structure of QFR from the anaerobic sulphate-reducing bacterium Desulfovibrio gigas (D. gigas) at 3.6 A resolution. The structure of the D. gigas QFR is a homo-dimer, each protomer comprising two hydrophilic subunits, A and B, and one transmembrane subunit C, together with six redox cofactors including two b-hemes. One menaquinone molecule is bound near heme bL in the hydrophobic subunit C. This location of the menaquinone-binding site differs from the menaquinol-binding cavity proposed previously for QFR from Wolinella succinogenes. The observed bound menaquinone might serve as an additional redox cofactor to mediate the proton-coupled electron transport across the membrane. Armed with these structural insights, we propose electron/proton-transfer pathways in the quinol reduction of fumarate to succinate in the D. gigas QFR.
Structural insights into the electron/proton transfer pathways in the quinol:fumarate reductase from Desulfovibrio gigas.,Guan HH, Hsieh YC, Lin PJ, Huang YC, Yoshimura M, Chen LY, Chen SK, Chuankhayan P, Lin CC, Chen NC, Nakagawa A, Chan SI, Chen CJ Sci Rep. 2018 Oct 8;8(1):14935. doi: 10.1038/s41598-018-33193-5. PMID:30297797[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Guan HH, Hsieh YC, Lin PJ, Huang YC, Yoshimura M, Chen LY, Chen SK, Chuankhayan P, Lin CC, Chen NC, Nakagawa A, Chan SI, Chen CJ. Structural insights into the electron/proton transfer pathways in the quinol:fumarate reductase from Desulfovibrio gigas. Sci Rep. 2018 Oct 8;8(1):14935. doi: 10.1038/s41598-018-33193-5. PMID:30297797 doi:http://dx.doi.org/10.1038/s41598-018-33193-5
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