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Poplar oxidoreductases involved in the oxidative stress response : a crystallographic snapshot towards the understanding of the catalytic mechanism

Abstract : Three oxidoreductases (glutathione peroxidase, GPX; thioredoxin, Trx and glutaredoxin, Grx) from Populus trichocarpa × deltoides (poplar tree) were characterized using X-ray crystallography approach. GPXs are a group of enzymes that regulate the levels of oxygen species in cells, and protect them against oxidative damage. In this study, I have determined the crystal structures of the reduced and oxidized form of poplar GPX5 (PtGPX5). 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. Trxs regulate various protein partners through the thiol-disulfide(s) reduction. The aim of this study is thus to precisely describe the catalytic mechanism of a new isoform of Trx, PtTrxh4, since it has been demonstrated recently to be reduced by Grx. PtTrxh4 contains three cysteines; one localized in an N-terminal extension (Cys4) and two in the usual Trx active site (WC1GPC2). Two crystal structures of PtTrxh4 solved in this study, wild-type and C61S mutant, allow us to propose a four-step disulfide cascade catalytic mechanism in accordance with enzymatic studies. Grxs are highly conserved redox-proteins that utilize electrons from GSH particularly to catalyze thiol-disulfide exchange reactions. Here, I present the structure of glutathionylated PtGrxS12, the first structure of plant Grx of subclass 1 with an atypical 28WCSYS32 active site. Protein structures solved here shed lights to our understanding of the redox mechanism in plant and to the enzyme-substrate interactions.
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Cha San Koh. Poplar oxidoreductases involved in the oxidative stress response : a crystallographic snapshot towards the understanding of the catalytic mechanism. Other. Université Henri Poincaré - Nancy 1, 2008. English. ⟨NNT : 2008NAN10028⟩. ⟨tel-01748531⟩

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