Cryo-crystallography of a true substrate, indole-3-glycerol phosphate, bound to a mutant (αD60N) tryptophan synthase α2β2 complex reveals the correct orientation of active site αGlu49

Journal of Biological Chemistry

Volumn 273, Issue 15, 1998, Pages 8553-8555

  Rhee, Sangkee ^a   Miles, Edith Wilson ^a   Davies, David R ^a,b  

^a NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

^b NATIONAL INSTITUTES OF HEALTH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; GLYCEROPHOSPHATE; INDOLE 3 GLYCEROL PHOSPHATE SYNTHASE; TRYPTOPHAN SYNTHASE;

ARTICLE; CRYSTALLOGRAPHY; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME MECHANISM; ENZYME STRUCTURE; NONHUMAN; PRIORITY JOURNAL; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; GLYCEROPHOSPHATES; MACROMOLECULAR SUBSTANCES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; POINT MUTATION; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; TRYPTOPHAN SYNTHASE;

BACTERIA (MICROORGANISMS);

EID: 0032502775     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.273.15.8553     Document Type: Article

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