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Publication Abstract from PubMed

Plastidial thioredoxin (TRX)-like2.1 proteins are atypical thioredoxins possessing a WCRKC active site signature and using glutathione for recycling. To obtain structural information supporting the peculiar catalytic mechanisms and target proteins of these TRXs, we solved the crystal structures of poplar TRX-like2.1 in oxidized and reduced states and of mutated variants. These structures share similar folding with TRXs exhibiting the canonical WCGPC signature. Moreover, the overall conformation is not altered by reduction of the catalytic disulfide bond or in a C45S/C67S variant that formed a disulfide-bridged dimer possibly mimicking reaction intermediates with target proteins. Modelling of the interaction of TRX-like2.1 with both NADPH- and ferredoxin-thioredoxin reductases indicates that the presence of Arg43 and Lys44 residues likely precludes reduction by the plastidial ferredoxin-thioredoxin reductase. This article is protected by copyright. All rights reserved.

Structural snapshots along the reaction mechanism of the atypical poplar thioredoxin-like2.1.,Chibani K, Saul F, Didierjean C, Rouhier N, Haouz A FEBS Lett. 2018 Feb 17. doi: 10.1002/1873-3468.13009. PMID:29453875^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.