Crystal structure of the bifunctional N-acetylglucosamine 1-phosphate uridyltransferase from Escherichia coli: A paradigm for the related pyrophosphorylase superfamily

EMBO Journal

Volumn 18, Issue 15, 1999, Pages 4096-4107

  Brown, Kieron ^a   Pompeo, Fredérique ^b   Dixon, Suzanne ^a   Mengin Lecreulx, Dominique ^b   Cambillau, Christian ^a   Bourne, Yves ^a  

^a Centre National de la Recherche Scientifique   (France)

^b CNRS   (France)

Author keywords

Acetyltransferase; Bifunctional; Crystallography; Drug design; Pyrophosphorylase

Indexed keywords

BACTERIAL ENZYME; HEXOSE 1 PHOSPHATE URIDYLYLTRANSFERASE; N ACETYLGLUCOSAMINE; OLIGOMER; PHOSPHORYLASE;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME CONFORMATION; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN QUATERNARY STRUCTURE; PROTEIN SECONDARY STRUCTURE; STRUCTURE ACTIVITY RELATION;

ACETYLTRANSFERASES; AMINO ACID SEQUENCE; BINDING SITES; ESCHERICHIA COLI; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; NUCLEOTIDYLTRANSFERASES; PROTEIN CONFORMATION; PROTEIN FOLDING; PYROPHOSPHATASES; SEQUENCE HOMOLOGY, AMINO ACID;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0033517131     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/18.15.4096     Document Type: Article

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