2p5q

<table><tr><td colspan='2'>[[2p5q]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Populus_balsamifera_subsp._trichocarpa_x_populus_deltoides Populus balsamifera subsp. trichocarpa x populus deltoides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P5Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2P5Q FirstGlance]. <br>

</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>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2p5r|2p5r]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PtGPX5 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3695 Populus balsamifera subsp. trichocarpa x Populus deltoides])</td></tr>

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== Publication Abstract from PubMed ==

Glutathione peroxidases (GPXs) are a group of enzymes that regulate the levels of reactive oxygen species in cells and tissues, and protect them against oxidative damage. Contrary to most of their counterparts in animal cells, the higher plant GPX homologues identified so far possess cysteine instead of selenocysteine in their active site. Interestingly, the plant GPXs are not dependent on glutathione but rather on thioredoxin as their in vitro electron donor. We have determined the crystal structures of the reduced and oxidized form of Populus trichocarpaxdeltoides GPX5 (PtGPX5), using a selenomethionine derivative. PtGPX5 exhibits an overall structure similar to that of the known animal GPXs. PtGPX5 crystallized in the assumed physiological dimeric form, displaying a pseudo ten-stranded beta sheet core. Comparison of both redox structures indicates that a drastic conformational change is necessary to bring the two distant cysteine residues together to form an intramolecular disulfide bond. In addition, a computer model of a complex of PtGPX5 and its in vitro recycling partner thioredoxin h1 is proposed on the basis of the crystal packing of the oxidized form enzyme. A possible role of PtGPX5 as a heavy-metal sink is also discussed.

Crystal structures of a poplar thioredoxin peroxidase that exhibits the structure of glutathione peroxidases: insights into redox-driven conformational changes.,Koh CS, Didierjean C, Navrot N, Panjikar S, Mulliert G, Rouhier N, Jacquot JP, Aubry A, Shawkataly O, Corbier C J Mol Biol. 2007 Jul 13;370(3):512-29. Epub 2007 Apr 19. PMID:17531267<ref>PMID:17531267</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 2p5q" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Populus balsamifera subsp. trichocarpa x populus deltoides]]

[[Category: Aubry, A]]

[[Category: Corbier, C]]

[[Category: Didierjean, C]]

[[Category: Jacquot, J P]]

[[Category: Koh, C S]]

[[Category: Mulliert, G]]

[[Category: Navrot, N]]

[[Category: Panjikar, S]]

[[Category: Rouhier, N]]

[[Category: Shawkataly, O]]

[[Category: Thioredoxin fold]]