PMID:11031118
| Citation |
Nordstrand, K, Sandström, A, Aslund, F, Holmgren, A, Otting, G and Berndt, KD (2000) NMR structure of oxidized glutaredoxin 3 from Escherichia coli. J. Mol. Biol. 303:423-32 |
|---|---|
| Abstract |
A high precision NMR structure of oxidized glutaredoxin 3 [C65Y] from Escherichia coli has been determined. The conformation of the active site including the disulphide bridge is highly similar to those in glutaredoxins from pig liver and T4 phage. A comparison with the previously determined structure of glutaredoxin 3 [C14S, C65Y] in a complex with glutathione reveals conformational changes between the free and substrate-bound form which includes the sidechain of the conserved, active site tyrosine residue. In the oxidized form this tyrosine is solvent exposed, while it adopts a less exposed conformation, stabilized by hydrogen bonds, in the mixed disulfide with glutathione. The structures further suggest that the formation of a covalent linkage between glutathione and glutaredoxin 3 is necessary in order to induce these structural changes upon binding of the glutathione peptide. This could explain the observed low affinity of glutaredoxins for S-blocked glutathione analogues, in spite of the fact that glutaredoxins are highly specific reductants of glutathione mixed disulfides. |
| Links |
PubMed Online version:10.1006/jmbi.2000.4145 |
| Keywords |
Amino Acid Sequence; Binding Sites; Conserved Sequence; Cysteine/metabolism; Disulfides/chemistry; Disulfides/metabolism; Escherichia coli/chemistry; Glutaredoxins; Glutathione/analogs & derivatives; Glutathione/metabolism; Glutathione/pharmacology; Hydrogen Bonding; Models, Molecular; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Oxidation-Reduction; Oxidoreductases; Oxygen/metabolism; Protein Binding; Protein Conformation/drug effects; Proteins/chemistry; Proteins/metabolism; Reducing Agents/metabolism; Reducing Agents/pharmacology; Sequence Alignment; Solvents; Substrate Specificity; Thermodynamics; Tyrosine/metabolism |
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