Crystal structure of Escherichia coli cytidine triphosphate synthetase, a nucleotide-regulated glutamine amidotransferase/ATP-dependent amidoligase fusion protein and homologue of anticancer and antiparasitic drug targets

Biochemistry

Volumn 43, Issue 21, 2004, Pages 6447-6463

  Endrizzi, James A ^a   Kim, Hanseong ^a   Anderson, Paul M ^b   Baldwin, Enoch P ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF MINNESOTA MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINETRIPHOSPHATE; CRYSTAL STRUCTURE; DIMERS; DRUG PRODUCTS; ESCHERICHIA COLI; HYDROLYSIS; MOLECULAR STRUCTURE; MONOMERS; MUTAGENESIS;

BIFUNCTIONAL MONOMERS; NUCLEOSIDES; TETRAMERS;

ENZYMES;

ADENOSINE TRIPHOSPHATE; ADENOSINE TRIPHOSPHATE DEPENDENT AMIDOLIGASE; AMIDOLIGASE; AMMONIA; BIOTIN DERIVATIVE; CYTIDINE TRIPHOSPHATE; CYTIDINE TRIPHOSPHATE SYNTHASE; DETHIOBIOTIN SYNTHETASE; DIMER; GLUTAMINE; GLUTAMINE AMIDOTRANSFERASE; GLUTAMINE PHENYLPYRUVATE AMINOTRANSFERASE; GUANINE NUCLEOTIDE; GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATE; HYBRID PROTEIN; LIGASE; MONOMER; NUCLEOTIDE; PYRIMIDINE; RIBONUCLEOTIDE TRIPHOSPHATE; SOLVENT; TETRAMER; TRANSFERASE; TYPE 1 GLUTAMINE AMIDOTRANFERASE; UNCLASSIFIED DRUG; URIDINE TRIPHOSPHATE;

ALLOSTERISM; AMIDOLIGASE N TERMINAL DOMAIN; ARTICLE; BINDING SITE; C TERMINAL DOMAIN; COMPETITIVE INHIBITION; CRYSTAL STRUCTURE; DRUG BINDING SITE; DRUG RESISTANCE; DRUG TARGETING; ENZYME ACTIVE SITE; ESCHERICHIA COLI; FEEDBACK SYSTEM; HOMOLOGY MODELING; HYDROLYSIS; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN INTERACTION; REGULATORY MECHANISM; SEQUENCE HOMOLOGY; TRIPHOSPHATE BINDING SITE;

AMINO ACID SEQUENCE; ANTINEOPLASTIC AGENTS; ANTIPARASITIC AGENTS; BINDING SITES; CARBON-NITROGEN LIGASES; CRYSTALLOGRAPHY, X-RAY; CYTIDINE TRIPHOSPHATE; ESCHERICHIA COLI PROTEINS; GLUTAMATE SYNTHASE; GUANOSINE TRIPHOSPHATE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEOTIDES; PROTEIN CONFORMATION; PROTEIN FOLDING; RECOMBINANT FUSION PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; STRUCTURAL HOMOLOGY, PROTEIN;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 2542604739     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0496945     Document Type: Article

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