5jab
From Proteopedia
(Difference between revisions)
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- | '''Unreleased structure''' | ||
- | + | ==Structure of the biliverdin reductase Rv2074 from Mycobacterium tuberculosis in complex with F420== | |
+ | <StructureSection load='5jab' size='340' side='right' caption='[[5jab]], [[Resolution|resolution]] 1.65Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[5jab]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JAB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JAB FirstGlance]. <br> | ||
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6J4:COENZYME+F420-3'>6J4</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=5jab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jab OCA], [http://pdbe.org/5jab PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jab RCSB], [http://www.ebi.ac.uk/pdbsum/5jab PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jab ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Bilirubin is a potent antioxidant that is produced from the reduction of the heme degradation product biliverdin. In mammalian cells and Cyanobacteria, NADH/NADPH-dependent biliverdin reductases (BVRs) of the Rossman-fold have been shown to catalyze this reaction. Here, we describe the characterization of Rv2074 from Mycobacterium tuberculosis, which belongs to a structurally and mechanistically distinct family of F420 H2 -dependent BVRs (F-BVRs) that are exclusively found in Actinobacteria. We have solved the crystal structure of Rv2074 bound to its cofactor, F420 , and used this alongside molecular dynamics simulations, site-directed mutagenesis and NMR spectroscopy to elucidate its catalytic mechanism. The production of bilirubin by Rv2074 could exploit the anti-oxidative properties of bilirubin and contribute to the range of immuno-evasive mechanisms that have evolved in M. tuberculosis to allow persistent infection. This article is protected by copyright. All rights reserved. | ||
- | + | Rv2074 is a novel F420 H2 -dependent biliverdin reductase in Mycobacterium tuberculosis.,Ahmed FH, Mohamed AE, Carr PD, Lee BM, Condic-Jurkic K, O'Mara ML, Jackson CJ Protein Sci. 2016 Jul 1. doi: 10.1002/pro.2975. PMID:27364382<ref>PMID:27364382</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
+ | <div class="pdbe-citations 5jab" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Ahmed, F H]] | ||
+ | [[Category: Carr, P D]] | ||
+ | [[Category: Jackson, C J]] | ||
+ | [[Category: Biliverdin reductase]] | ||
+ | [[Category: F420 binding protein]] | ||
+ | [[Category: Flavin/deazaflavin oxidoreductase]] | ||
+ | [[Category: Oxidoreductase]] | ||
+ | [[Category: Split beta-barrel fold]] |
Revision as of 11:46, 14 July 2016
Structure of the biliverdin reductase Rv2074 from Mycobacterium tuberculosis in complex with F420
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