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[[Image:1qlb.gif|left|200px]]<br />
<applet load="1qlb" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1qlb, resolution 2.33&Aring;" />
'''RESPIRATORY COMPLEX II-LIKE FUMARATE REDUCTASE FROM WOLINELLA SUCCINOGENES'''<br />


==Overview==
==respiratory complex II-like fumarate reductase from Wolinella succinogenes==
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, ... [[http://ispc.weizmann.ac.il/pmbin/getpm?10586875 (full description)]]
<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 [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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.33&#8491;</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='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 ==
[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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ql/1qlb_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1qlb ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.


==About this Structure==
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<ref>PMID:10586875</ref>
1QLB is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Wolinella_succinogenes Wolinella succinogenes]] with CA, HEM, FES, F3S, SF4, FAD, FMR and LMT as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[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]]. Structure known Active Sites: FA1, FA2, FS1, FS2, FS3, FS4, FS5, FS6, HE1 and HE2. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QLB OCA]].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10586875 10586875]
</div>
[[Category: Protein complex]]
<div class="pdbe-citations 1qlb" style="background-color:#fffaf0;"></div>
[[Category: Succinate dehydrogenase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Wolinella succinogenes]]
[[Category: Wolinella succinogenes]]
[[Category: Auer, M.]]
[[Category: Auer M]]
[[Category: Kroeger, A.]]
[[Category: Kroeger A]]
[[Category: Lancaster, C.R.D.]]
[[Category: Lancaster CRD]]
[[Category: Michel, H.]]
[[Category: Michel H]]
[[Category: CA]]
[[Category: F3S]]
[[Category: FAD]]
[[Category: FES]]
[[Category: FMR]]
[[Category: HEM]]
[[Category: LMT]]
[[Category: SF4]]
[[Category: citric acid cycle]]
[[Category: dihaem cytochrome b]]
[[Category: flavoprotein]]
[[Category: fumarate reductase]]
[[Category: iron-sulphur protein]]
[[Category: respiratory chain]]
[[Category: succinate dehydrogenase]]
 
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