1qo8
From Proteopedia
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| - | [[Image:1qo8.gif|left|200px]]<br /> | ||
| - | <applet load="1qo8" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1qo8, resolution 2.15Å" /> | ||
| - | '''THE STRUCTURE OF THE OPEN CONFORMATION OF A FLAVOCYTOCHROME C3 FUMARATE REDUCTASE'''<br /> | ||
| - | == | + | ==The structure of the open conformation of a flavocytochrome c3 fumarate reductase== |
| - | Fumarate reductases and succinate dehydrogenases play central roles in the | + | <StructureSection load='1qo8' size='340' side='right'caption='[[1qo8]], [[Resolution|resolution]] 2.15Å' scene=''> |
| + | == 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> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15Å</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> | ||
| + | <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> | ||
| + | == Function == | ||
| + | [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 == | ||
| + | [[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/qo/1qo8_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=1qo8 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1qo8" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Flavocytochrome 3D structures|Flavocytochrome 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Shewanella frigidimarina]] | ||
| + | [[Category: Bamford V]] | ||
| + | [[Category: Dobbin PS]] | ||
| + | [[Category: Hemmings AM]] | ||
| + | [[Category: Richardson DJ]] | ||
Current revision
The structure of the open conformation of a flavocytochrome c3 fumarate reductase
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