The structure of apo tryptophanase from Escherichia coli reveals a wide-open conformation

Acta Crystallographica Section D: Biological Crystallography

Volumn 63, Issue 9, 2007, Pages 969-974

  Tsesin, Natalia ^a   Kogan, Anna ^a   Gdalevsky, Garik Y ^a   Himanen, Juha Pekka ^b   Cohen Luria, Rivka ^a   Parola, Abraham H ^a   Goldgur, Yehuda ^a,b   Almog, Orna ^a  

^a BEN GURION UNIVERSITY OF THE NEGEV   (Israel)

^b MEMORIAL SLOAN KETTERING CANCER CENTER   (United States)

Author keywords

PLP dependent enzymes; Tryptophanase

Indexed keywords

ESCHERICHIA COLI PROTEIN; TRYPTOPHANASE;

ARTICLE; BINDING SITE; CATALYSIS; CHEMICAL STRUCTURE; CHEMISTRY; CRYSTALLIZATION; ENZYME SPECIFICITY; ENZYMOLOGY; ESCHERICHIA COLI; GENETICS; METABOLISM; METHODOLOGY; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; PROTEUS VULGARIS; X RAY CRYSTALLOGRAPHY;

BINDING SITES; CATALYSIS; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; MODELS, MOLECULAR; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEUS VULGARIS; SUBSTRATE SPECIFICITY; TRYPTOPHANASE;

ESCHERICHIA COLI; PROTEUS VULGARIS;

EID: 34548336959     PISSN: 09074449     EISSN: 13990047     Source Type: Journal    
DOI: 10.1107/S0907444907036396     Document Type: Article

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