1xvq

<StructureSection load='1xvq' size='340' side='right' caption='[[1xvq]], [[Resolution|resolution]] 1.75&Aring;' scene=''>

<table><tr><td colspan='2'>[[1xvq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XVQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XVQ FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene>, <scene name='pdbligand=YT3:YTTRIUM+(III)+ION'>YT3</scene></td></tr>

<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSX:S-OXY+CYSTEINE'>CSX</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tpx ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</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=1xvq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xvq OCA], [http://pdbe.org/1xvq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xvq RCSB], [http://www.ebi.ac.uk/pdbsum/1xvq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1xvq ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/TPX_MYCTU TPX_MYCTU]] Has antioxidant activity. Could remove peroxides or H(2)O(2) (By similarity).

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

A thiol peroxidase (Tpx) from Mycobacterium tuberculosis was functionally analyzed. The enzyme shows NADPH-linked peroxidase activity using a thioredoxin-thioredoxin reductase system as electron donor, and anti-oxidant activity in a thiol-dependent metal-catalyzed oxidation system. It reduces H2O2, t-butyl hydroperoxide, and cumene hydroperoxide, and is inhibited by sulfhydryl reagents. Mutational studies revealed that the peroxidatic (Cys60) and resolving (Cys93) cysteine residues are critical amino acids for catalytic activity. The X-ray structure determined to a resolution of 1.75 A shows a thioredoxin fold similar to that of other peroxiredoxin family members. Superposition with structural homologues in oxidized and reduced forms indicates that the M. tuberculosis Tpx is a member of the atypical two-Cys peroxiredoxin family. In addition, the short distance that separates the Calpha atoms of Cys60 and Cys93 and the location of these cysteine residues in unstructured regions may indicate that the M. tuberculosis enzyme is oxidized, though the side-chain of Cys60 is poorly visible. It is solely in the reduced Streptococcus pneumoniae Tpx structure that both residues are part of two distinct helical segments. The M. tuberculosis Tpx is dimeric both in solution and in the crystal structure. Amino acid residues from both monomers delineate the active site pocket.

Functional and structural characterization of a thiol peroxidase from Mycobacterium tuberculosis.,Rho BS, Hung LW, Holton JM, Vigil D, Kim SI, Park MS, Terwilliger TC, Pedelacq JD J Mol Biol. 2006 Sep 1;361(5):850-63. Epub 2006 Jun 27. PMID:16884737<ref>PMID:16884737</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1xvq" style="background-color:#fffaf0;"></div>

*[[Thiol peroxidase|Thiol peroxidase]]

[[Category: Holton, J M]]

[[Category: Hung, L W]]

[[Category: Kim, S I]]

[[Category: Park, M S]]

[[Category: Pedelacq, J D]]

[[Category: Rho, B S]]

[[Category: Structural genomic]]

[[Category: Terwilliger, T C]]

[[Category: Vigil, D]]

[[Category: Oxidoreductase]]

[[Category: Thioredoxin fold]]