Thioredoxin and peptide methionine sulfoxide reductase: Convergence of similar structure and function in distinct structural folds

Proteins: Structure, Function and Genetics

Volumn 46, Issue 2, 2002, Pages 149-152

  Gladyshev, Vadim N ^a  

^a UNIVERSITY OF NEBRASKA LINCOLN   (United States)

Author keywords

CxxC motif; Fold; Peptide methionine sulfoxide reductase; Reaction mechanism; Redox; Structure; Thioredoxin

Indexed keywords

CYSTEINE; OXIDOREDUCTASE; PEPTIDE METHIONINE SULFOXIDE REDUCTASE; THIOREDOXIN; UNCLASSIFIED DRUG;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ANTIOXIDANT ACTIVITY; ARTICLE; ENZYME ACTIVE SITE; ENZYME CONFORMATION; MOLECULAR EVOLUTION; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; REGULATORY MECHANISM; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; EVOLUTION, MOLECULAR; MOLECULAR SEQUENCE DATA; OXIDATION-REDUCTION; OXIDOREDUCTASES; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ANALYSIS, PROTEIN; STRUCTURE-ACTIVITY RELATIONSHIP; THIOREDOXIN;

EID: 0036467162     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.10003     Document Type: Article

References (16)

1. Thioredoxin structure and mechanism: Conformational changes on oxidation of the active-site sulfhydryls to a disulfide
2. Recent trends in glutathione biochemistry - Glutathione-protein interactions: A molecular link between oxidative stress and cell proliferation?
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4. Methionine residues may protect proteins from critical oxidative damage
5. Thioredoxin - A fold for all reasons
6. Modulation of potassium channel function by methionine oxidation and reduction
7. Overexpression of peptide-methionine sulfoxide reductase in Saccharomyces cerevisiae and human T cells provides them with high resistance to oxidative stress
8. Crystal structure of the Escherichia coli peptide methionine sulphoxide reductase at 1.9 Å resolution
9. Structure and mechanism of peptide methionine sulfoxide reductase, an "antioxidation" enzyme
10. A sulfenic acid enzyme intermediate is involved in the catalytic mechanism of peptide methionine sulfoxide reductase from Escherichia coli
11. Thiol-disulfide exchange is involved in the catalytic mechanism of peptide methionine sulfoxide reductase
12. Identification and characterization of a putative active site for peptide methionine sulfoxide reductase (MsrA) and its substrate stereospecificity
13. Crystal structure of a novel human peroxidase enzyme at 2.0 Å resolution
14. Protein structure comparison by alignment of distance matrices
15. A family of novel peroxidases, peroxiredoxins
16. Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate