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2wdv
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 2wdv is ON HOLD until Paper Publication Authors: Ruprecht, J., Yankovskaya, V., Maklashina, E., Iwata, S., Cecchini, G. Description: E. coli succin...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==E. coli succinate:quinone oxidoreductase (SQR) with an empty quinone- binding pocket== | |
| + | <StructureSection load='2wdv' size='340' side='right'caption='[[2wdv]], [[Resolution|resolution]] 3.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2wdv]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WDV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WDV FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=TEO:MALATE+LIKE+INTERMEDIATE'>TEO</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2wdq|2wdq]], [[2wdr|2wdr]], [[1nek|1nek]], [[1nen|1nen]], [[2acz|2acz]]</div></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_(quinone) Succinate dehydrogenase (quinone)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.5.1 1.3.5.1] </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=2wdv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wdv OCA], [https://pdbe.org/2wdv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wdv RCSB], [https://www.ebi.ac.uk/pdbsum/2wdv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wdv ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/DHSD_ECOLI DHSD_ECOLI]] Membrane-anchoring subunit of succinate dehydrogenase (SDH). [[https://www.uniprot.org/uniprot/DHSA_ECOLI DHSA_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. [[https://www.uniprot.org/uniprot/DHSC_ECOLI DHSC_ECOLI]] Membrane-anchoring subunit of succinate dehydrogenase (SDH). [[https://www.uniprot.org/uniprot/DHSB_ECOLI DHSB_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. | ||
| + | == 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/wd/2wdv_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=2wdv ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 2wdv" style="background-color:#fffaf0;"></div> | ||
| - | + | ==See Also== | |
| + | *[[Succinate Dehydrogenase|Succinate Dehydrogenase]] | ||
| + | *[[Succinate dehydrogenase 3D structures|Succinate dehydrogenase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bacillus coli migula 1895]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Cecchini, G]] | ||
| + | [[Category: Iwata, S]] | ||
| + | [[Category: Maklashina, E]] | ||
| + | [[Category: Ruprecht, J]] | ||
| + | [[Category: Yankovskaya, V]] | ||
| + | [[Category: Cell inner membrane]] | ||
| + | [[Category: Electron transport]] | ||
| + | [[Category: Flavoprotein]] | ||
| + | [[Category: Metal-binding]] | ||
| + | [[Category: Oxidoreductase]] | ||
| + | [[Category: Succinate dehydrogenase activity]] | ||
| + | [[Category: Transmembrane]] | ||
| + | [[Category: Tricarboxylic acid cycle]] | ||
Current revision
E. coli succinate:quinone oxidoreductase (SQR) with an empty quinone- binding pocket
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