View source for 2lqo


==Mrx1 reduced==
<StructureSection load='2lqo' size='340' side='right'caption='[[2lqo]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2lqo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LQO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LQO FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2lqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lqo OCA], [https://pdbe.org/2lqo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lqo RCSB], [https://www.ebi.ac.uk/pdbsum/2lqo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lqo ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Y3198_MYCTU Y3198_MYCTU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
To survive hostile conditions, the bacterial pathogen Mycobacterium tuberculosis produces millimolar concentrations of mycothiol as a redox buffer against oxidative stress. The reductases that couple the reducing power of mycothiol to redox active proteins in the cell are not known. We report a novel mycothiol-dependent reductase (mycoredoxin-1) with a CGYC catalytic motif. With mycoredoxin-1 and mycothiol deletion strains of Mycobacterium smegmatis, we show that mycoredoxin-1 and mycothiol are involved in the protection against oxidative stress. Mycoredoxin-1 acts as an oxidoreductase exclusively linked to the mycothiol electron transfer pathway and it can reduce S-mycothiolated mixed disulphides. Moreover, we solved the solution structures of oxidized and reduced mycoredoxin-1, revealing a thioredoxin fold with a putative mycothiol-binding site. With HSQC snapshots during electron transport, we visualize the reduction of oxidized mycoredoxin-1 as a function of time and find that mycoredoxin-1 gets S-mycothiolated on its N-terminal nucleophilic cysteine. Mycoredoxin-1 has a redox potential of -218 mV and hydrogen bonding with neighbouring residues lowers the pK(a) of its N-terminal nucleophilic cysteine. Determination of the oxidized and reduced structures of mycoredoxin-1, better understanding of mycothiol-dependent reactions in general, will likely give new insights in how M. tuberculosis survives oxidative stress in human macrophages.

Mycoredoxin-1 is one of the missing links in the oxidative stress defence mechanism of Mycobacteria.,Van Laer K, Buts L, Foloppe N, Vertommen D, Van Belle K, Wahni K, Roos G, Nilsson L, Mateos LM, Rawat M, van Nuland NA, Messens J Mol Microbiol. 2012 Sep 13. doi: 10.1111/mmi.12030. PMID:22970802<ref>PMID:22970802</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2lqo" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Buts L]]
[[Category: Messens J]]
[[Category: Van Laer K]]