5jab: Difference between revisions

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'''Unreleased structure'''


The entry 5jab is ON HOLD  until Paper Publication
==Structure of the biliverdin reductase Rv2074 from Mycobacterium tuberculosis in complex with F420==
<StructureSection load='5jab' size='340' side='right' caption='[[5jab]], [[Resolution|resolution]] 1.65&Aring;' 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.


Authors:  
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>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</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]]
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