View source for 3lt3


==Crystal structure of Rv3671c from M. tuberculosis H37Rv, Ser343Ala mutant, inactive form==
<StructureSection load='3lt3' size='340' side='right'caption='[[3lt3]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3lt3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LT3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LT3 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</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=3lt3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lt3 OCA], [https://pdbe.org/3lt3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lt3 RCSB], [https://www.ebi.ac.uk/pdbsum/3lt3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lt3 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Y3671_MYCTU Y3671_MYCTU] Required for M.tuberculosis resistance to oxidative stress in addition to its role in resistance to acid, which is essential for virulence. It protects M.tuberculosis against phagolysosomal concentrations of acid and maintains its intrabacterial pH when phagocytosed by IFN-gamma-activated macrophages.<ref>PMID:18641659</ref> <ref>PMID:20947023</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Rv3671c, a putative serine protease, is crucial for persistence of Mycobacterium tuberculosis in the hostile environment of the phagosome. We show that Rv3671c is required for M. tuberculosis resistance to oxidative stress in addition to its role in protection from acidification. Structural and biochemical analyses demonstrate that the periplasmic domain of Rv3671c is a functional serine protease of the chymotrypsin family and, remarkably, that its activity increases on oxidation. High-resolution crystal structures of this protease in an active strained state and in an inactive relaxed state reveal that a solvent-exposed disulfide bond controls the protease activity by constraining two distant regions of Rv3671c and stabilizing it in the catalytically active conformation. In vitro biochemical studies confirm that activation of the protease in an oxidative environment is dependent on this reversible disulfide bond. These results suggest that the disulfide bond modulates activity of Rv3671c depending on the oxidative environment in vivo.

Structural insight into serine protease Rv3671c that Protects M. tuberculosis from oxidative and acidic stress.,Biswas T, Small J, Vandal O, Odaira T, Deng H, Ehrt S, Tsodikov OV Structure. 2010 Oct 13;18(10):1353-63. PMID:20947023<ref>PMID:20947023</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3lt3" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mycobacterium tuberculosis H37Rv]]
[[Category: Biswas T]]
[[Category: Ehrt S]]
[[Category: Small J]]
[[Category: Tsodikov OV]]
[[Category: Vandal O]]