|
|
| Line 1: |
Line 1: |
| - | ==Crystal structure of Plasmodium falciparum dihydroorotate dehydrogenase bound with Inhibitor DSM59==
| + | #REDIRECT [[5del]] This PDB entry is obsolete and replaced by 5del |
| - | <StructureSection load='4ryh' size='340' side='right' caption='[[4ryh]], [[Resolution|resolution]] 2.30Å' scene=''>
| + | |
| - | == Structural highlights ==
| + | |
| - | <table><tr><td colspan='2'>[[4ryh]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RYH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RYH 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=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=4ryh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ryh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ryh RCSB], [http://www.ebi.ac.uk/pdbsum/4ryh 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 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>
| + | |
| - | == References ==
| + | |
| - | <references/>
| + | |
| - | __TOC__
| + | |
| - | </StructureSection>
| + | |
| - | [[Category: Deng, X]]
| + | |
| - | [[Category: Phillips, M]]
| + | |
| - | [[Category: Alpha/beta barrel]]
| + | |
| - | [[Category: Fmn]]
| + | |
| - | [[Category: Mitochondrial membrane]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Oxidoreductase-oxidoreductase inhibitor complex]]
| + | |
