Structures of open (R) and close (T) states of prephenate dehydratase (PDT)-Implication of allosteric regulation by l-phenylalanine

Journal of Structural Biology

Volumn 162, Issue 1, 2008, Pages 94-107

  Tan, Kemin ^a   Li, Hui ^a   Zhang, Rongguang ^a   Gu, Minyi ^a   Clancy, Shonda T ^a   Joachimiak, Andrzej ^a  

^a Structural Biology Center   (United States)

Author keywords

ACT domain; Allosteric regulation; l Phe binding; PDT domain; Prephenate dehydratase structure

Indexed keywords

DIMER; PHENYLALANINE; PREPHENATE DEHYDRATASE;

ALLOSTERISM; AMINO TERMINAL SEQUENCE; ARTICLE; CATALYSIS; CHLOROBIUM; CHLOROBIUM TEPIDUM; CRYSTAL STRUCTURE; ENZYME ANALYSIS; ENZYME CONFORMATION; ENZYME REGULATION; ENZYME STRUCTURE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; STAPHYLOCOCCUS AUREUS; STRUCTURE ACTIVITY RELATION;

ALLOSTERIC REGULATION; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CHLOROBIUM; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; PHENYLALANINE; PREPHENATE DEHYDRATASE; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID; STAPHYLOCOCCUS AUREUS;

CHLOROBACULUM TEPIDUM; STAPHYLOCOCCUS AUREUS;

EID: 41849090791     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2007.11.009     Document Type: Article

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