View source for 6vpd


==Crystal structure of Trgpx in apo form==
<StructureSection load='6vpd' size='340' side='right'caption='[[6vpd]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6vpd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichoderma_reesei_QM6a Trichoderma reesei QM6a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VPD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VPD 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]] 2.603&#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=6vpd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vpd OCA], [https://pdbe.org/6vpd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vpd RCSB], [https://www.ebi.ac.uk/pdbsum/6vpd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vpd ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/G0RHF8_HYPJQ G0RHF8_HYPJQ] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Glutathione peroxidases (GPx) are a family of enzymes with the ability to reduce organic and inorganic hydroperoxides to the corresponding alcohols using glutathione or thioredoxin as an electron donor. Here, we report the functional and structural characterization of a GPx identified in Trichoderma reesei (TrGPx). TrGPx was recombinantly expressed in a bacterial host and purified using affinity. Using a thioredoxin coupled assay, TrGPx exhibited activity of 28 U and 12.5 U in the presence of the substrates H2O2 and t-BOOH, respectively, and no activity was observed when glutathione was used. These results indicated that TrGPx is a thioredoxin peroxidase and hydrolyses H2O2 better than t-BOOH. TrGPx kinetic parameters using a pyrogallol assay resulted at Kmapp = 11.7 mM, Vmaxapp = 10.9 IU/mug TrGPx, kcat = 19 s(-1) and a catalytic efficiency of 1.6 mM(-1) s(-1) to H2O2 as substrate. Besides that, TrGPx demonstrated an optimum pH ranging from 9.0-12.0 and a half-life of 36 min at 80 degrees C. TrGPx 3D-structure was obtained in a reduced state and non-catalytic conformation. The overall fold is similar to the other phospholipid-hydroperoxide glutathione peroxidases. These data contribute to understand the antioxidant mechanism in fungi and provide information for using antioxidant enzymes in biotechnological applications.

Structural and functional characterization of the glutathione peroxidase-like thioredoxin peroxidase from the fungus Trichoderma reesei.,Adriani PP, de Paiva FCR, de Oliveira GS, Leite AC, Sanches AS, Lopes AR, Dias MVB, Chambergo FS Int J Biol Macromol. 2020 Nov 29;167:93-100. doi: 10.1016/j.ijbiomac.2020.11.179. PMID:33259843<ref>PMID:33259843</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6vpd" style="background-color:#fffaf0;"></div>

==See Also==
*[[Glutathione peroxidase|Glutathione peroxidase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Trichoderma reesei QM6a]]
[[Category: Adriani PP]]
[[Category: Chambergo FS]]
[[Category: De Oliveira GS]]
[[Category: Dias MVB]]
[[Category: Paiva FCR]]