NMR structure of oxidized glutaredoxin 3 from Escherichia coli.
J Mol Biol
; 303(3): 423-32, 2000 Oct 27.
Article
em En
| MEDLINE
| ID: mdl-11031118
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.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Contexto em Saúde:
3_ND
Problema de saúde:
3_neglected_diseases
/
3_zoonosis
Assunto principal:
Oxirredutases
/
Proteínas
/
Ressonância Magnética Nuclear Biomolecular
/
Escherichia coli
Idioma:
En
Revista:
J Mol Biol
Ano de publicação:
2000
Tipo de documento:
Article
País de afiliação:
Suécia