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Volumn 278, Issue 52, 2003, Pages 52826-52833
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Crystal structure of wild-type penicillin-binding protein 5 from Escherichia coli: Implications for deacylation of the acyl-enzyme complex
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Author keywords
[No Author keywords available]
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Indexed keywords
ACYLATION;
ANTIBIOTICS;
CRYSTAL STRUCTURE;
ENZYMES;
ESCHERICHIA COLI;
HYDROGEN BONDS;
HYDROLYSIS;
MUTAGENESIS;
CELL WALL;
MUTATIONS;
BIOCHEMISTRY;
ACYL COENZYME A;
ASPARAGINE;
ASPARTIC ACID;
BACTERIAL PROTEIN;
BETA LACTAM ANTIBIOTIC;
GLYCINE;
PENICILLIN BINDING PROTEIN;
PENICILLIN BINDING PROTEIN 5;
SERINE;
UNCLASSIFIED DRUG;
AMINO ACID SUBSTITUTION;
ARTICLE;
COMPLEX FORMATION;
CONTROLLED STUDY;
CRYSTAL STRUCTURE;
DEACYLATION;
ENZYME ACTIVE SITE;
ENZYME ACTIVITY;
ESCHERICHIA COLI;
GENE MUTATION;
HYDROGEN BOND;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN BINDING;
PROTEIN HYDROLYSIS;
PROTEIN MOTIF;
PROTEIN STRUCTURE;
STRUCTURE ANALYSIS;
AMINO ACID MOTIFS;
BACTERIAL PROTEINS;
BINDING SITES;
CARRIER PROTEINS;
CRYSTALLOGRAPHY, X-RAY;
ESCHERICHIA COLI;
GENE DELETION;
HEXOSYLTRANSFERASES;
HYDROGEN BONDING;
HYDROLYSIS;
KINETICS;
LYSINE;
MODELS, MOLECULAR;
MURAMOYLPENTAPEPTIDE CARBOXYPEPTIDASE;
MUTATION;
PENICILLIN-BINDING PROTEINS;
PEPTIDYL TRANSFERASES;
PROTEIN BINDING;
PROTEIN CONFORMATION;
PROTEIN STRUCTURE, TERTIARY;
X-RAY DIFFRACTION;
BACTERIA (MICROORGANISMS);
ESCHERICHIA COLI;
NEGIBACTERIA;
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EID: 0347362788
PISSN: 00219258
EISSN: None
Source Type: Journal
DOI: 10.1074/jbc.M310177200 Document Type: Article |
Times cited : (80)
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References (37)
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