PMID:11080639
| Citation |
Tête-Favier, F, Cobessi, D, Boschi-Muller, S, Azza, S, Branlant, G and Aubry, A (2000) Crystal structure of the Escherichia coli peptide methionine sulphoxide reductase at 1.9 A resolution. Structure 8:1167-78 |
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| Abstract |
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. |
| Links | |
| Keywords |
Amino Acid Sequence; Bacterial Proteins/chemistry; Binding Sites; Catalysis; Crystallography, X-Ray; Cysteine/chemistry; Escherichia coli/enzymology; Evolution, Molecular; Methionine Sulfoxide Reductases; Models, Molecular; Molecular Sequence Data; Oxidoreductases/chemistry; Protein Conformation; Protein Folding; Protein Structure, Tertiary; Recombinant Fusion Proteins/chemistry; Selenomethionine/chemistry; Sequence Alignment; Sequence Homology, Amino Acid; Species Specificity; Structure-Activity Relationship |
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