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1qo8

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1qo8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Shewanella_frigidimarina Shewanella frigidimarina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QO8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QO8 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1qo8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Shewanella_frigidimarina Shewanella frigidimarina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QO8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QO8 FirstGlance]. <br>
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</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=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15&#8491;</td></tr>
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<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>
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<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=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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=1qo8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qo8 OCA], [https://pdbe.org/1qo8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qo8 RCSB], [https://www.ebi.ac.uk/pdbsum/1qo8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qo8 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=1qo8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qo8 OCA], [https://pdbe.org/1qo8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qo8 RCSB], [https://www.ebi.ac.uk/pdbsum/1qo8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qo8 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/FRD2_SHEFN FRD2_SHEFN]] Catalyzes unidirectional fumarate reduction using artificial electron donors such as methyl viologen. The physiological reductant is unknown.
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[https://www.uniprot.org/uniprot/FRD2_SHEFN FRD2_SHEFN] Catalyzes unidirectional fumarate reduction using artificial electron donors such as methyl viologen. The physiological reductant is unknown.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1qo8 ConSurf].
</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=1qo8 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Fumarate reductases and succinate dehydrogenases play central roles in the metabolism of eukaryotic and prokaryotic cells. A recent medium resolution structure of the Escherichia coli fumarate reductase (Frd) has revealed the overall organization of the membrane-bound complex. Here we present the first high resolution X-ray crystal structure of a water-soluble bacterial fumarate reductase in an open conformation. This structure reveals a mobile domain that modulates substrate access to the active site and provides new insights into the mechanism of this widespread and important family of FAD-containing respiratory proteins.
 
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Open conformation of a flavocytochrome c3 fumarate reductase.,Bamford V, Dobbin PS, Richardson DJ, Hemmings AM Nat Struct Biol. 1999 Dec;6(12):1104-7. PMID:10581549<ref>PMID:10581549</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1qo8" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[Flavocytochrome 3D structures|Flavocytochrome 3D structures]]
*[[Flavocytochrome 3D structures|Flavocytochrome 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Shewanella frigidimarina]]
[[Category: Shewanella frigidimarina]]
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[[Category: Succinate dehydrogenase]]
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[[Category: Bamford V]]
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[[Category: Bamford, V]]
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[[Category: Dobbin PS]]
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[[Category: Dobbin, P S]]
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[[Category: Hemmings AM]]
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[[Category: Hemmings, A M]]
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[[Category: Richardson DJ]]
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[[Category: Richardson, D J]]
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[[Category: Oxidoreductase]]
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Revision as of 06:05, 17 April 2024

The structure of the open conformation of a flavocytochrome c3 fumarate reductase

PDB ID 1qo8

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