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Volumn 8, Issue 11, 2000, Pages 1167-1178
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Crystal structure of the Escherichia coli peptide methionine sulphoxide reductase at 1.9 Å resolution
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Author keywords
Catalytic cysteine residue; MAD; MsrA; Peptide methionine sulphoxide reductase; roll
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Indexed keywords
BACTERIAL ENZYME;
CYSTEINE;
METHIONINE SULFOXIDE REDUCTASE;
UNCLASSIFIED DRUG;
AMINO TERMINAL SEQUENCE;
ANALYTIC METHOD;
ARTICLE;
CARBOXY TERMINAL SEQUENCE;
CATALYSIS;
CRYSTAL STRUCTURE;
ENZYME ANALYSIS;
ENZYME STRUCTURE;
ESCHERICHIA COLI;
GENETIC PROCEDURES;
OPTICAL RESOLUTION;
PRIORITY JOURNAL;
AMINO ACID SEQUENCE;
BACTERIAL PROTEINS;
BINDING SITES;
CATALYSIS;
CRYSTALLOGRAPHY, X-RAY;
CYSTEINE;
ESCHERICHIA COLI;
EVOLUTION, MOLECULAR;
MODELS, MOLECULAR;
MOLECULAR SEQUENCE DATA;
OXIDOREDUCTASES;
PROTEIN CONFORMATION;
PROTEIN FOLDING;
PROTEIN STRUCTURE, TERTIARY;
RECOMBINANT FUSION PROTEINS;
SELENOMETHIONINE;
SEQUENCE ALIGNMENT;
SEQUENCE HOMOLOGY, AMINO ACID;
SPECIES SPECIFICITY;
STRUCTURE-ACTIVITY RELATIONSHIP;
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EID: 0034435463
PISSN: 09692126
EISSN: None
Source Type: Journal
DOI: 10.1016/S0969-2126(00)00526-8 Document Type: Article |
Times cited : (84)
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References (50)
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