7P9E

Chlamydomonas reinhardtii NADPH Dependent Thioredoxin Reductase 1 domain CS mutant

Summary for 7P9E

• Entry DOI: 10.2210/pdb7p9e/pdb
• Descriptor: Thioredoxin reductase, FLAVIN-ADENINE DINUCLEOTIDE, 1-ETHOXY-2-(2-ETHOXYETHOXY)ETHANE, ... (4 entities in total)
• Functional Keywords: oxidoreductase, flavoprotein, fad binding domain
• Biological source: Chlamydomonas reinhardtii
• Total number of polymer chains: 2
• Total formula weight: 106789.37

Authors

Fuesser, F.,Kuemmel, D. (deposition date: 2021-07-27, release date: 2022-01-19, Last modification date: 2024-01-31)

Primary citation

Marchetti, G.M.,Fusser, F.,Singh, R.K.,Brummel, M.,Koch, O.,Kummel, D.,Hippler, M.
Structural analysis revealed a novel conformation of the NTRC reductase domain from Chlamydomonas reinhardtii.
J.Struct.Biol., 214:107829-107829, 2021

PubMed Abstract: In plant chloroplasts, thiol regulation is driven by two systems. One relies on the activity of thioredoxins through their light dependent reduction by ferredoxin via a ferredoxin-thioredoxin reductase (FTR). In the other system, a NADPH-dependent redox regulation is driven by a NADPH-thioredoxin reductase C (NTRC). While the thioredoxin system has been deeply studied, a more thorough understanding of the function of this plant specific NTRC is desirable. NTRC is a single polypeptide harbouring a thioredoxin domain (Trx) at the C-terminus of a NADPH-dependent Thioredoxin reductase (TrxR). To provide functional and structural insights, we studied the crystal structure of the TrxR domain of the NTRC from Chlamydomonas reinhardtii (CrNTRC, Cre01.g054150.t1.2) and its Cys136Ser (C136S) mutant, which is characterized by the mutation of the resolving cysteine in the active site of the TrxR domain. Furthermore, we confirmed the role of NTRC as electron donor for 2-Cys peroxiredoxin (PRX) also in C. reinhardtii. The structural data of TrxR were employed to develop a scheme of action which addresses electron transfer between TrxR and Trx of NTRC and between NTRC and its substrates.

PubMed: 34974142
DOI: 10.1016/j.jsb.2021.107829

Experimental method

X-RAY DIFFRACTION (2.36 Å)