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| | ==QUINOL:FUMARATE REDUCTASE FROM WOLINELLA SUCCINOGENES== | | ==QUINOL:FUMARATE REDUCTASE FROM WOLINELLA SUCCINOGENES== |
| - | <StructureSection load='2bs2' size='340' side='right' caption='[[2bs2]], [[Resolution|resolution]] 1.78Å' scene=''> | + | <StructureSection load='2bs2' size='340' side='right'caption='[[2bs2]], [[Resolution|resolution]] 1.78Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2bs2]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Wolinella_succinogenes Wolinella succinogenes]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1qla 1qla]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BS2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BS2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2bs2]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Wolinella_succinogenes Wolinella succinogenes]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1qla 1qla]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BS2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BS2 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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=NA:SODIUM+ION'>NA</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]] 1.78Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1e7p|1e7p]], [[1qlb|1qlb]], [[2bs3|2bs3]], [[2bs4|2bs4]]</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=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></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 Succinate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.99.1 1.3.99.1] </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=2bs2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bs2 OCA], [https://pdbe.org/2bs2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bs2 RCSB], [https://www.ebi.ac.uk/pdbsum/2bs2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bs2 ProSAT]</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=2bs2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bs2 OCA], [http://pdbe.org/2bs2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bs2 RCSB], [http://www.ebi.ac.uk/pdbsum/2bs2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2bs2 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/FRDA_WOLSU FRDA_WOLSU]] The fumarate reductase enzyme complex is required for fumarate respiration using formate or sulfide as electron donor. [[http://www.uniprot.org/uniprot/FRDC_WOLSU FRDC_WOLSU]] The fumarate reductase enzyme complex is required for fumarate respiration using formate or sulfide as electron donor. [[http://www.uniprot.org/uniprot/FRDB_WOLSU FRDB_WOLSU]] The fumarate reductase enzyme complex is required for fumarate respiration using formate or sulfide as electron donor. | + | [https://www.uniprot.org/uniprot/FRDA_WOLSU FRDA_WOLSU] The fumarate reductase enzyme complex is required for fumarate respiration using formate or sulfide as electron donor. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Succinate dehydrogenase]] | + | [[Category: Large Structures]] |
| | [[Category: Wolinella succinogenes]] | | [[Category: Wolinella succinogenes]] |
| - | [[Category: Lancaster, C R.D]] | + | [[Category: Lancaster CRD]] |
| - | [[Category: Citric acid cycle]]
| + | |
| - | [[Category: Iron-sulphur protein]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Respiratory chain]]
| + | |
| Structural highlights
2bs2 is a 6 chain structure with sequence from Wolinella succinogenes. This structure supersedes the now removed PDB entry 1qla. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.78Å |
| Ligands: | , , , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
FRDA_WOLSU The fumarate reductase enzyme complex is required for fumarate respiration using formate or sulfide as electron donor.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Membrane protein complexes can support both the generation and utilisation of a transmembrane electrochemical proton potential ('proton-motive force'), either by transmembrane electron transfer coupled to protolytic reactions on opposite sides of the membrane or by transmembrane proton transfer. Here we provide the first evidence that both of these mechanisms are combined in the case of a specific respiratory membrane protein complex, the dihaem-containing quinol:fumarate reductase (QFR) of Wolinella succinogenes, so as to facilitate transmembrane electron transfer by transmembrane proton transfer. We also demonstrate the non-functionality of this novel transmembrane proton transfer pathway ('E-pathway') in a variant QFR where a key glutamate residue has been replaced. The 'E-pathway', discussed on the basis of the 1.78-Angstrom-resolution crystal structure of QFR, can be concluded to be essential also for the viability of pathogenic varepsilon-proteobacteria such as Helicobacter pylori and is possibly relevant to proton transfer in other dihaem-containing membrane proteins, performing very different physiological functions.
Evidence for transmembrane proton transfer in a dihaem-containing membrane protein complex.,Madej MG, Nasiri HR, Hilgendorff NS, Schwalbe H, Lancaster CR EMBO J. 2006 Oct 18;25(20):4963-70. Epub 2006 Oct 5. PMID:17024183[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Madej MG, Nasiri HR, Hilgendorff NS, Schwalbe H, Lancaster CR. Evidence for transmembrane proton transfer in a dihaem-containing membrane protein complex. EMBO J. 2006 Oct 18;25(20):4963-70. Epub 2006 Oct 5. PMID:17024183
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