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2wdq

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{{Seed}}
 
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[[Image:2wdq.png|left|200px]]
 
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==E. coli succinate:quinone oxidoreductase (SQR) with carboxin bound==
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The line below this paragraph, containing "STRUCTURE_2wdq", creates the "Structure Box" on the page.
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<StructureSection load='2wdq' size='340' side='right'caption='[[2wdq]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2wdq]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WDQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WDQ FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.4&#8491;</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=CBE:2-METHYL-N-PHENYL-5,6-DIHYDRO-1,4-OXATHIINE-3-CARBOXAMIDE'>CBE</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=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TEO:MALATE+LIKE+INTERMEDIATE'>TEO</scene></td></tr>
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{{STRUCTURE_2wdq| PDB=2wdq | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2wdq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wdq OCA], [https://pdbe.org/2wdq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wdq RCSB], [https://www.ebi.ac.uk/pdbsum/2wdq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wdq ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SDHA_ECOLI SDHA_ECOLI] Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth.<ref>PMID:24374335</ref> <ref>PMID:12560550</ref> <ref>PMID:16407191</ref> <ref>PMID:19710024</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wd/2wdq_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=2wdq ConSurf].
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<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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Three new structures of Escherichia coli succinate-quinone oxidoreductase (SQR) have been solved. One with the specific quinone-binding site (Q-site) inhibitor carboxin present has been solved at 2.4 A resolution and reveals how carboxin inhibits the Q-site. The other new structures are with the Q-site inhibitor pentachlorophenol and with an empty Q-site. These structures reveal important details unresolved in earlier structures. Comparison of the new SQR structures shows how subtle rearrangements of the quinone-binding site accommodate the different inhibitors. The position of conserved water molecules near the quinone binding pocket leads to a reassessment of possible water-mediated proton uptake networks that complete reduction of ubiquinone. The dicarboxylate-binding site in the soluble domain of SQR is highly similar to that seen in high resolution structures of avian SQR (PDB 2H88) and soluble flavocytochrome c (PDB 1QJD) showing mechanistically significant structural features conserved across prokaryotic and eukaryotic SQRs.
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===E. COLI SUCCINATE:QUINONE OXIDOREDUCTASE (SQR) WITH CARBOXIN BOUND===
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Structure of Escherichia coli succinate:quinone oxidoreductase with an occupied and empty quinone-binding site.,Ruprecht J, Yankovskaya V, Maklashina E, Iwata S, Cecchini G J Biol Chem. 2009 Oct 23;284(43):29836-46. Epub 2009 Aug 25. PMID:19710024<ref>PMID:19710024</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 2wdq" style="background-color:#fffaf0;"></div>
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==About this Structure==
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==See Also==
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2WDQ is a 12 chains structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WDQ OCA].
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*[[Succinate Dehydrogenase|Succinate Dehydrogenase]]
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*[[Succinate dehydrogenase 3D structures|Succinate dehydrogenase 3D structures]]
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==Reference==
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== References ==
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<ref group="xtra">PMID:19710024</ref><references group="xtra"/>
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<references/>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Cecchini, G.]]
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[[Category: Large Structures]]
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[[Category: Iwata, S.]]
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[[Category: Cecchini G]]
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[[Category: Maklashina, E.]]
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[[Category: Iwata S]]
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[[Category: Ruprecht, J.]]
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[[Category: Maklashina E]]
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[[Category: Yankovskaya, V.]]
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[[Category: Ruprecht J]]
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[[Category: 2fe-2]]
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[[Category: Yankovskaya V]]
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[[Category: 3fe-4]]
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[[Category: 4fe-4]]
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[[Category: Acetylation]]
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[[Category: Cell inner membrane]]
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[[Category: Cell membrane]]
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[[Category: Electron transport]]
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[[Category: Fad]]
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[[Category: Flavoprotein]]
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[[Category: Heme]]
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[[Category: Iron]]
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[[Category: Iron-sulfur]]
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[[Category: Membrane]]
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[[Category: Metal-binding]]
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[[Category: Oxidoreductase]]
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[[Category: Succinate dehydrogenase activity]]
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[[Category: Transmembrane]]
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[[Category: Transport]]
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[[Category: Tricarboxylic acid cycle]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Sep 21 16:39:39 2009''
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Current revision

E. coli succinate:quinone oxidoreductase (SQR) with carboxin bound

PDB ID 2wdq

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