1H75

Structural basis for the thioredoxin-like activity profile of the glutaredoxin-like protein NrdH-redoxin from Escherichia coli.

1H75 の概要

• エントリーDOI: 10.2210/pdb1h75/pdb
• 分子名称: GLUTAREDOXIN-LIKE PROTEIN NRDH (2 entities in total)
• 機能のキーワード: electron transport, nrdh, thioredoxin, glutaredoxin, redox protein
• 由来する生物種: ESCHERICHIA COLI
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9152.47

構造登録者

Stehr, M.,Schneider, G.,Aslund, F.,Holmgren, A.,Lindqvist, Y. (登録日: 2001-07-03, 公開日: 2001-08-09, 最終更新日: 2024-10-23)

主引用文献

Stehr, M.,Schneider, G.,Aslund, F.,Holmgren, A.,Lindqvist, Y.
Structural Basis for the Thioredoxin-Like Activity Profile of the Glutaredoxin-Like Nrdh-Redoxin from Escherichia Coli
J.Biol.Chem., 276:35836-, 2001

PubMed Abstract: NrdH-redoxin is a representative of a class of small redox proteins that contain a conserved CXXC motif and are characterized by a glutaredoxin-like amino acid sequence and thioredoxin-like activity profile. The crystal structure of recombinant Escherichia coli NrdH-redoxin in the oxidized state has been determined at 1.7 A resolution by multiwavelength anomalous diffraction. NrdH-redoxin belongs to the thioredoxin superfamily and is structurally most similar to E. coli glutaredoxin 3 and phage T4 glutaredoxin. The angle between the C-terminal helix alpha3 and strand beta4, which differs between thioredoxin and glutaredoxin, has an intermediate value in NrdH-redoxin. The orientation of this helix is to a large extent determined by an extended hydrogen-bond network involving the highly conserved sequence motif (61)WSGFRP(D/E)(67), which is unique to this subclass of the thioredoxin superfamily. Residues that bind glutathione in glutaredoxins are in general not conserved in NrdH-redoxin, and no glutathione-binding cleft is present. Instead, NrdH-redoxin contains a wide hydrophobic pocket at the surface, similar to thioredoxin. Modeling studies suggest that NrdH-redoxin can interact with E. coli thioredoxin reductase at this pocket and also via a loop that is complementary to a crevice in the reductase in a similar manner as observed in the E. coli thioredoxin-thioredoxin reductase complex.

PubMed: 11441020
DOI: 10.1074/JBC.M105094200

実験手法

X-RAY DIFFRACTION (1.7 Å)