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1qlb

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Revision as of 09:58, 15 September 2021

respiratory complex II-like fumarate reductase from Wolinella succinogenes

Structural highlights

1qlb is a 6 chain structure with sequence from Wolinella succinogenes. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , , , , ,
Related:	1qla, 1fum
Activity:	Succinate dehydrogenase, with EC number 1.3.99.1
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. [FRDC_WOLSU] The fumarate reductase enzyme complex is required for fumarate respiration using formate or sulfide as electron donor. [FRDB_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

Fumarate reductase couples the reduction of fumarate to succinate to the oxidation of quinol to quinone, in a reaction opposite to that catalysed by the related complex II of the respiratory chain (succinate dehydrogenase). Here we describe the crystal structure at 2.2 A resolution of the three protein subunits containing fumarate reductase from the anaerobic bacterium Wolinella succinogenes. Subunit A contains the site of fumarate reduction and a covalently bound flavin adenine dinucleotide prosthetic group. Subunit B contains three iron-sulphur centres. The menaquinol-oxidizing subunit C consists of five membrane-spanning, primarily helical segments and binds two haem b molecules. On the basis of the structure, we propose a pathway of electron transfer from the dihaem cytochrome b to the site of fumarate reduction and a mechanism of fumarate reduction. The relative orientations of the soluble and membrane-embedded subunits of succinate:quinone oxidoreductases appear to be unique.

Structure of fumarate reductase from Wolinella succinogenes at 2.2 A resolution.,Lancaster CR, Kroger A, Auer M, Michel H Nature. 1999 Nov 25;402(6760):377-85. PMID:10586875^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Lancaster CR, Kroger A, Auer M, Michel H. Structure of fumarate reductase from Wolinella succinogenes at 2.2 A resolution. Nature. 1999 Nov 25;402(6760):377-85. PMID:10586875 doi:10.1038/46483

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1qlb"

@@ Line 3: / Line 3: @@
 <StructureSection load='1qlb' size='340' side='right'caption='[[1qlb]], [[Resolution|resolution]] 2.33&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1qlb]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Wolinella_succinogenes Wolinella succinogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QLB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QLB FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1qlb]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Wolinella_succinogenes Wolinella succinogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QLB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QLB FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <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=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
+</td></tr><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=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=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1qla|1qla]], [[1fum|1fum]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1qla|1qla]], [[1fum|1fum]]</div></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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Succinate_dehydrogenase Succinate dehydrogenase], with EC number [https://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qlb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qlb OCA], [http://pdbe.org/1qlb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qlb RCSB], [http://www.ebi.ac.uk/pdbsum/1qlb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qlb 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=1qlb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qlb OCA], [https://pdbe.org/1qlb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qlb RCSB], [https://www.ebi.ac.uk/pdbsum/1qlb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qlb ProSAT]</span></td></tr>
 </table>
 == 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. [[https://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. [[https://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.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1qlb

From Proteopedia

Revision as of 09:58, 15 September 2021

respiratory complex II-like fumarate reductase from Wolinella succinogenes

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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