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Volumn 19, Issue 24, 2000, Pages 6652-6663
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The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate thymidylyltransferase (RmlA)
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Author keywords
Drug design; Nucleotidyltransferase; Pseudomonas aeruginosa; Pyrophosphorylase; Rhamnose
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Indexed keywords
BACTERIAL ENZYME;
GLUCOSE 1 PHOSPHATE THYMIDYLTRANSFERASE;
MEMBRANE PROTEIN;
NUCLEOTIDYLTRANSFERASE;
RHAMNOSE;
THYMIDINE DERIVATIVE;
THYMIDINE DIPHOSPHATE;
UNCLASSIFIED DRUG;
ARTICLE;
BACTERIAL CELL WALL;
CARBOHYDRATE SYNTHESIS;
CATALYSIS;
COMPLEX FORMATION;
CONTROLLED STUDY;
DIMERIZATION;
DRUG DESIGN;
DRUG TARGETING;
ENZYME STRUCTURE;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN DOMAIN;
PSEUDOMONAS AERUGINOSA;
REGULATORY MECHANISM;
STRUCTURE ACTIVITY RELATION;
AMINO ACID SEQUENCE;
ANIMALS;
BINDING SITES;
CAENORHABDITIS ELEGANS;
CATALYSIS;
CLONING, MOLECULAR;
CRYSTALLOGRAPHY, X-RAY;
ESCHERICHIA COLI;
MODELS, MOLECULAR;
MOLECULAR SEQUENCE DATA;
MUTAGENESIS, SITE-DIRECTED;
NUCLEOSIDE DIPHOSPHATE SUGARS;
NUCLEOTIDYLTRANSFERASES;
PROTEIN STRUCTURE, SECONDARY;
PROTEIN SUBUNITS;
PSEUDOMONAS AERUGINOSA;
RECOMBINANT PROTEINS;
SEQUENCE ALIGNMENT;
SEQUENCE HOMOLOGY, AMINO ACID;
THYMINE NUCLEOTIDES;
BACTERIA (MICROORGANISMS);
PSEUDOMONAS;
PSEUDOMONAS AERUGINOSA;
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EID: 0034671801
PISSN: 02614189
EISSN: None
Source Type: Journal
DOI: 10.1093/emboj/19.24.6652 Document Type: Article |
Times cited : (165)
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References (57)
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