5xur
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==Crystal Structure of Rv2466c C22S Mutant== | |
+ | <StructureSection load='5xur' size='340' side='right' caption='[[5xur]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[5xur]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XUR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XUR FirstGlance]. <br> | ||
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></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=5xur FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xur OCA], [http://pdbe.org/5xur PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xur RCSB], [http://www.ebi.ac.uk/pdbsum/5xur PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xur ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/TRLR_MYCTU TRLR_MYCTU]] In vitro, the reduced form of Rv2466c catalyzes the reduction and activation of TP053, which is a thienopyrimidine derivative drug that can kill both replicating and non-replicating M.tuberculosis.<ref>PMID:24877756</ref> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The success of Mycobacterium tuberculosis (Mtb) as a pathogen depends on the redundant and complex mechanisms it has evolved for resisting nitrosative and oxidative stresses inflicted by host immunity. Improving our understanding of these defense pathways can reveal vulnerable points in Mtb pathogenesis. In this study, we combined genetic, structural, computational, biochemical, and biophysical approaches to identify a novel enzyme class represented by Rv2466c. We show that Rv2466c is a mycothiol-dependent nitroreductase of Mtb and can reduce the nitro group of a novel mycobactericidal compound using mycothiol as a cofactor. In addition to its function as a nitroreductase, Rv2466c confers partial protection to menadione stress. | ||
- | + | Identification of a Mycothiol-Dependent Nitroreductase from Mycobacterium tuberculosis.,Negri A, Javidnia P, Mu R, Zhang X, Vendome J, Gold B, Roberts J, Barman D, Ioerger T, Sacchettini JC, Jiang X, Burns-Huang K, Warrier T, Ling Y, Warren JD, Oren DA, Beuming T, Wang H, Wu J, Li H, Rhee KY, Nathan CF, Liu G, Somersan-Karakaya S ACS Infect Dis. 2018 Feb 21. doi: 10.1021/acsinfecdis.7b00111. PMID:29465985<ref>PMID:29465985</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
+ | <div class="pdbe-citations 5xur" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Li, H]] | ||
+ | [[Category: Zhang, X]] | ||
+ | [[Category: Oxidoreductase]] | ||
+ | [[Category: Thioredoxin-like]] |
Revision as of 06:26, 14 March 2018
Crystal Structure of Rv2466c C22S Mutant
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