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5del
From Proteopedia
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| - | ''' | + | ==Crystal structure of Plasmodium falciparum dihydroorotate dehydrogenase bound with Inhibitor DSM59== |
| + | <StructureSection load='5del' size='340' side='right' caption='[[5del]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5del]] is a 1 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4ryh 4ryh]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DEL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DEL FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=D59:N-(3,5-DICHLOROPHENYL)-2-METHYL-3-NITROBENZAMIDE'>D59</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>, <scene name='pdbligand=ORO:OROTIC+ACID'>ORO</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydroorotate_dehydrogenase_(quinone) Dihydroorotate dehydrogenase (quinone)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.5.2 1.3.5.2] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5del FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5del OCA], [http://pdbe.org/5del PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5del RCSB], [http://www.ebi.ac.uk/pdbsum/5del PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/PYRD_PLAF7 PYRD_PLAF7]] Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Plasmodium species are protozoan parasites that are the causative agent of malaria. Malaria is a devastating disease, and its treatment and control have been hampered by the propensity of the parasite to become drug-resistant. Dihydroorotate dehydrogenase (DHODH) has been identified as a promising new target for the development of antimalarial agents. Here, the X-ray structure of P. falciparum DHODH bound to a potent and selective N-phenylbenzamide-based inhibitor (DSM59) is described at 2.3 A resolution. The structure elucidates novel binding-site interactions and shows how conformational flexibility of the enzyme leads to the ability to bind diverse chemical structures with high affinity. This information provides new insight into the design of high-affinity DHODH inhibitors for the treatment of malaria. | ||
| - | The | + | The X-ray structure of Plasmodium falciparum dihydroorotate dehydrogenase bound to a potent and selective N-phenylbenzamide inhibitor reveals novel binding-site interactions.,Deng X, Matthews D, Rathod PK, Phillips MA Acta Crystallogr F Struct Biol Commun. 2015 May;71(Pt 5):553-9. doi:, 10.1107/S2053230X15000989. Epub 2015 Apr 21. PMID:25945708<ref>PMID:25945708</ref> |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5del" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Deng, X]] | [[Category: Deng, X]] | ||
[[Category: Phillips, M]] | [[Category: Phillips, M]] | ||
| + | [[Category: Alpha/beta barrel]] | ||
| + | [[Category: Fmn]] | ||
| + | [[Category: Mitochondrial membrane]] | ||
| + | [[Category: Oxidoreductase-oxidoreductase inhibitor complex]] | ||
Revision as of 13:40, 7 October 2015
Crystal structure of Plasmodium falciparum dihydroorotate dehydrogenase bound with Inhibitor DSM59
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