5nyk

Crystal structure of the atypical poplar thioredoxin-like2.1 in oxidized state

spinqualitylabelsall models 5nyk, resolution 1.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5nyk is a 1 chain structure with sequence from Populus tremula x Populus tremuloides. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.05Å Ligands: CL, K, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function I0BZV0_POPPZ 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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