5NYM

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

Summary for 5NYM

• Entry DOI: 10.2210/pdb5nym/pdb
• Related: 5NYK 5NYL 5NYN 5NYO
• Descriptor: Thioredoxin-like protein 2.1, CHLORIDE ION, POTASSIUM ION, ... (5 entities in total)
• Functional Keywords: atypical thioredoxin, disulfide exchange, oxidoreductase
• Biological source: Populus tremula x Populus tremuloides
• Total number of polymer chains: 1
• Total formula weight: 14361.39

Authors

Chibani, K.,Saul, F.A.,Haouz, A.,Rouhier, N. (deposition date: 2017-05-11, release date: 2018-02-28, Last modification date: 2024-05-01)

Primary citation

Chibani, K.,Saul, F.,Didierjean, C.,Rouhier, N.,Haouz, A.
Structural snapshots along the reaction mechanism of the atypical poplar thioredoxin-like2.1.
FEBS Lett., 592:1030-1041, 2018

PubMed Abstract: 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. Modeling of the interaction of TRX-like2.1 with both NADPH- and ferredoxin-thioredoxin reductases (FTR) indicates that the presence of Arg43 and Lys44 residues likely precludes reduction by the plastidial FTR.

PubMed: 29453875
DOI: 10.1002/1873-3468.13009

Experimental method

X-RAY DIFFRACTION (1.4 Å)