7P9D

Crystal structure of Chlamydomonas reinhardtii NADPH Dependent Thioredoxin Reductase 1 domain

7P9D の概要

• エントリーDOI: 10.2210/pdb7p9d/pdb
• 分子名称: Thioredoxin reductase, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total)
• 機能のキーワード: oxidoreductase, flavoprotein, fad binding domain
• 由来する生物種: Chlamydomonas reinhardtii (Chlamydomonas smithii)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 53248.52

構造登録者

Singh, R.K.,Marchetti, G.M.,Hippler, M.,Kuemmel, D. (登録日: 2021-07-27, 公開日: 2022-01-12, 最終更新日: 2024-10-23)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.99 Å)