1DBY

NMR STRUCTURES OF CHLOROPLAST THIOREDOXIN M CH2 FROM THE GREEN ALGA CHLAMYDOMONAS REINHARDTII

1DBY の概要

• エントリーDOI: 10.2210/pdb1dby/pdb
• 関連するPDBエントリー: 1TOF
• 分子名称: CHLOROPLAST THIOREDOXIN M CH2 (1 entity in total)
• 機能のキーワード: thioredoxin m, thioredoxin ch2, chloroplastic thioredoxin, oxidoreductase
• 由来する生物種: Chlamydomonas reinhardtii
• 細胞内の位置: Plastid, chloroplast (By similarity): P23400
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11686.55

構造登録者

Lancelin, J.-M.,Guilhaudis, L.,Krimm, I.,Blackledge, M.J.,Marion, D. (登録日: 1999-11-03, 公開日: 1999-11-08, 最終更新日: 2024-10-16)

主引用文献

Lancelin, J.M.,Guilhaudis, L.,Krimm, I.,Blackledge, M.J.,Marion, D.,Jacquot, J.P.
NMR structures of thioredoxin m from the green alga Chlamydomonas reinhardtii.
Proteins, 41:334-349, 2000

PubMed Abstract: Chloroplast thioredoxin m from the green alga Chlamydomomas reinhardtii is very efficiently reduced in vitro and in vivo in the presence of photoreduced ferredoxin and a ferredoxin dependent ferredoxin-thioredoxin reductase. Once reduced, thioredoxin m has the capability to quickly activate the NADP malate dehydrogenase (EC 1.1.1.82) a regulatory enzyme involved in an energy-dependent assimilation of carbon dioxide in C4 plants. This activation is the result of the reduction of two disulfide bridges by thioredoxin m, that are located at the N- and C-terminii of the NADP malate dehydrogenase. The molecular structure of thioredoxin m was solved using NMR and compared to other known thioredoxins. Thioredoxin m belongs to the prokaryotic type of thioredoxin, which is divergent from the eukaryotic-type thioredoxins also represented in plants by the h (cytosolic) and f (chloroplastic) types of thioredoxins. The dynamics of the molecule have been assessed using (15)N relaxation data and are found to correlate well with regions of disorder found in the calculated NMR ensemble. The results obtained provide a novel basis to interpret the thioredoxin dependence of the activation of chloroplast NADP-malate dehydrogenase. The specific catalytic mechanism that takes place in the active site of thioredoxins is also discussed on the basis of the recent new understanding and especially in the light of the dual general acid-base catalysis exerted on the two cysteines of the redox active site. It is proposed that the two cysteines of the redox active site may insulate each other from solvent attack by specific packing of invariable hydrophobic amino acids.

PubMed: 11025545
DOI: 10.1002/1097-0134(20001115)41:3<334::AID-PROT60>3.3.CO;2-D

実験手法

SOLUTION NMR