1H75
Structural basis for the thioredoxin-like activity profile of the glutaredoxin-like protein NrdH-redoxin from Escherichia coli.
Summary for 1H75
| Entry DOI | 10.2210/pdb1h75/pdb |
| Descriptor | GLUTAREDOXIN-LIKE PROTEIN NRDH (2 entities in total) |
| Functional Keywords | electron transport, nrdh, thioredoxin, glutaredoxin, redox protein |
| Biological source | ESCHERICHIA COLI |
| Total number of polymer chains | 1 |
| Total formula weight | 9152.47 |
| Authors | Stehr, M.,Schneider, G.,Aslund, F.,Holmgren, A.,Lindqvist, Y. (deposition date: 2001-07-03, release date: 2001-08-09, Last modification date: 2024-10-23) |
| Primary citation | 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 Cited by 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: 11441020DOI: 10.1074/JBC.M105094200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
Download full validation report
