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Titolo:
Crystal structure of the Escherichia coli peptide methionine sulphoxide reductase at 1.9 angstrom resolution
Autore:
Tete-Favier, F; Cobessi, D; Boschi-Muller, S; Azza, S; Branlant, G; Aubry, A;
Indirizzi:
Univ Henri Poincare, Lab Cristallog & Modelisat Mat Mineraux & Biol, Grp Biocristallog, F-54506 Vandoeuvre Nancy, France Univ Henri Poincare Vandoeuvre Nancy France F-54506 oeuvre Nancy, France Univ Henri Poincare, Lab Maturat ARN & Enzymol Mol, F-54506 Vandoeuvre Nancy, France Univ Henri Poincare Vandoeuvre Nancy France F-54506 oeuvre Nancy, France
Titolo Testata:
STRUCTURE
fascicolo: 11, volume: 8, anno: 2000,
pagine: 1167 - 1178
SICI:
0969-2126(20001115)8:11<1167:CSOTEC>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
X-RAY-DIFFRACTION; SULFOXIDE REDUCTASE; OXIDATIVE DAMAGE; ENZYMATIC REDUCTION; ACTIVE-SITE; GENE; EXPRESSION; IDENTIFICATION; RESIDUES; PROTEINS;
Keywords:
peptide methionine sulphoxide reductase; MsrA; MAD; alpha/beta roll; catalytic cysteine residue;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
50
Recensione:
Indirizzi per estratti:
Indirizzo: Aubry, A Univ Henri Poincare, Lab Cristallog & Modelisat Mat Mineraux & Biol, Grp Biocristallog, BP239, F-54506 Vandoeuvre Nancy, France Univ Henri Poincare BP239 Vandoeuvre Nancy France F-54506 France
Citazione:
F. Tete-Favier et al., "Crystal structure of the Escherichia coli peptide methionine sulphoxide reductase at 1.9 angstrom resolution", STRUCTURE, 8(11), 2000, pp. 1167-1178

Abstract

Background: Peptide methionine sulphoxide reductases catalyze the reduction of oxidized methionine residues in proteins. They are implicated in the defense of organisms against oxidative stress and in the regulation of processes involving peptide methionine oxidation/reduction. These enzymes are found in numerous organisms, from bacteria to mammals and plants. Their primary structure shows no significant similarity to any other known protein. Results: The X-ray structure of the peptide methionine sulphoxide reductase from Escherichia coli was determined at 3 Angstrom resolution by the multiple wavelength anomalous dispersion method for the selenomethionine-substituted enzyme, and it was refined to 1.9 Angstrom resolution for the native enzyme. The 23 kDa protein is folded into an alpha/beta roll and contains alarge proportion of coils. Among the three cysteine residues involved in the catalytic mechanism, Cys-51 is positioned at the N terminus of an a helix, in a solvent-exposed area composed of highly conserved amino acids. The two others, Cys-198 and Cys-206, are located in the C-terminal coil. Conclusions: Sequence alignments show that the overall fold of the peptidemethionine sulphoxide reductase from E. coli is likely to be conserved in many species. The characteristics observed in the Cys-51 environment are inagreement with the expected accessibility of the active site of an enzyme that reduces methionine sulphoxides in various proteins. (Cys-51 could be activated by the influence of an a helix dipole. The involvement of the two other cysteine residues in the catalytic mechanism requires a movement of the C-terminal coil. Several conserved amino acids and water molecules are discussed as potential participants in the reaction.

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Documento generato il 09/07/20 alle ore 01:33:50