View source for 1y25


==structure of mycobacterial thiol peroxidase Tpx==
<StructureSection load='1y25' size='340' side='right'caption='[[1y25]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1y25]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y25 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y25 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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></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=1y25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y25 OCA], [https://pdbe.org/1y25 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y25 RCSB], [https://www.ebi.ac.uk/pdbsum/1y25 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y25 ProSAT], [https://www.topsan.org/Proteins/TBSGC/1y25 TOPSAN]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TPX_MYCTU TPX_MYCTU] Has antioxidant activity. Could remove peroxides or H(2)O(2) (By similarity).
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/y2/1y25_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1y25 ConSurf].
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== Publication Abstract from PubMed ==
The genome of Mycobacterium tuberculosis encodes several peroxiredoxins (Prxs) thought to be active against organic and inorganic peroxides. The open reading frame Rv1932 encodes a 165-residue thiol peroxidase (Tpx), which belongs to the atypical 2-Cys peroxiredoxin family. The crystal structure of the C60S mutant of M. tuberculosis Tpx (MtTpx) crystallized in space group P3(1)21, with unit-cell parameters a = 106.08, b = 106.08, c = 65.33 A. The structure has been refined to an R value of 17.1% (R(free) = 24.9%) at 2.1 A resolution. MtTpx is structurally homologous to other peroxiredoxins, including the mycobacterial AhpC and AhpE. The inactive MtTpx C60S mutant structure closely resembles the structure of Streptococcus pneumoniae Tpx (SpTpx) and thus represents the reduced enzyme state. The mutated active-site serine is electrostatically linked to Arg130 and hydrogen bonded to Thr57, practically identical to the cysteine in SpTpx. A cocrystallized acetate molecule mimics the position of the substrate and interacts with Ser60, Arg130 and Thr57.

Structure of the inactive variant C60S of Mycobacterium tuberculosis thiol peroxidase.,Stehr M, Hecht HJ, Jager T, Flohe L, Singh M Acta Crystallogr D Biol Crystallogr. 2006 May;62(Pt 5):563-7. Epub 2006, Apr 19. PMID:16627951<ref>PMID:16627951</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 1y25" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Hecht HJ]]
[[Category: Hoffmann B]]
[[Category: Jger T]]
[[Category: Singh M]]
[[Category: Stehr M]]