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Structural analysis revealed a novel conformation of the NTRC reductase domain from Chlamydomonas reinhardtii.

Authors :
Marchetti, Giulia Maria
Füsser, Friederike
Singh, Rohit Kumar
Brummel, Monika
Koch, Oliver
Kümmel, Daniel
Hippler, Michael
Source :
Journal of Structural Biology. Mar2022, Vol. 214 Issue 1, pN.PAG-N.PAG. 1p.
Publication Year :
2022

Abstract

• CrNTRC can donate electrons to 2-Cys Peroxiredoxin1 in vitro. • CrNTRC reductase domain is characterized by a peculiar conformation, which was previously only described in Methanosarcina mazei. • The reductase domain of C136S mutant of CrNTRC is in the F O conformation. 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. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
10478477
Volume :
214
Issue :
1
Database :
Academic Search Index
Journal :
Journal of Structural Biology
Publication Type :
Academic Journal
Accession number :
155631858
Full Text :
https://doi.org/10.1016/j.jsb.2021.107829