7t6c
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==E. coli dihydroorotate dehydrogenase bound to the ubiquinone surrogate DCIP== | |
| + | <StructureSection load='7t6c' size='340' side='right'caption='[[7t6c]], [[Resolution|resolution]] 2.53Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7t6c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7T6C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7T6C 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]] 2.53Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ORO:OROTIC+ACID'>ORO</scene>, <scene name='pdbligand=PE4:2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL'>PE4</scene>, <scene name='pdbligand=RLM:2,6-BIS(CHLORANYL)-4-[(4-HYDROXYPHENYL)AMINO]PHENOL'>RLM</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=7t6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7t6c OCA], [https://pdbe.org/7t6c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7t6c RCSB], [https://www.ebi.ac.uk/pdbsum/7t6c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7t6c ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PYRD_ECOLI PYRD_ECOLI] Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.<ref>PMID:10074342</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Hydroxyalkylquinolines (HAQs) are ubiquitious natural products but their interactions with associated protein targets remain elusive. We report X-ray crystal structures of two HAQs in complex with dihydroorotate dehydrogenase (DHODH). Our results reveal the structural basis of DHODH inhibition by HAQs and open the door to downstream structure-activity relationship studies. | ||
| - | + | Structural insights into inhibition of the drug target dihydroorotate dehydrogenase by bacterial hydroxyalkylquinolines.,Horwitz SM, Blue TC, Ambarian JA, Hoshino S, Seyedsayamdost MR, Davis KM RSC Chem Biol. 2022 Feb 7;3(4):420-425. doi: 10.1039/d1cb00255d. eCollection 2022, Apr 6. PMID:35441142<ref>PMID:35441142</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 7t6c" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Dihydroorotate dehydrogenase 3D structures|Dihydroorotate dehydrogenase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli K-12]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Ambarian JA]] | ||
| + | [[Category: Davis KM]] | ||
| + | [[Category: Horwitz SM]] | ||
Current revision
E. coli dihydroorotate dehydrogenase bound to the ubiquinone surrogate DCIP
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