D221 in thymidylate synthase controls conformation change, and thereby opening of the imidazolidine

Biochemistry

Volumn 37, Issue 39, 1998, Pages 13893-13901

  Sage, Carleton R ^a,b   Michelitsch, Melissa D ^a   Stout, Thomas J ^a,b   Biermann, Donna ^a   Nissen, Robert ^a   Finer Moore, Janet ^a   Stroud, Robert M ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b MetaXen   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

IMIDAZOLINE; THYMIDYLATE SYNTHASE;

ARTICLE; CRYSTAL STRUCTURE; DNA SEQUENCE; DNA SYNTHESIS; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ESCHERICHIA COLI; HYDROGEN BOND; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL;

ASPARAGINE; ASPARTIC ACID; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; FLUORODEOXYURIDYLATE; FOLIC ACID; HYDROGEN BONDING; IMIDAZOLES; MACROMOLECULAR SUBSTANCES; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN BINDING; PROTEIN CONFORMATION; QUINAZOLINES; SUBSTRATE SPECIFICITY; TETRAHYDROFOLATES; THYMIDYLATE SYNTHASE;

ESCHERICHIA COLI;

EID: 0032578430     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9810510     Document Type: Article

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