A flexible loop at the dimer interface is a part of the active site of the adjacent monomer of Escherichia coli orotate phosphoribosyltransferase

Biochemistry

Volumn 35, Issue 12, 1996, Pages 3803-3809

  Henriksen, Anette ^a   Aghajari, Nushin ^a   Jensen, Kaj Frank ^a   Gajhede, Michael ^a  

^a UNIVERSITY OF COPENHAGEN   (Denmark)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE PHOSPHATE; BACTERIAL ENZYME; DIMER; GUANOSINE PHOSPHATE; HYPOXANTHINE PHOSPHORIBOSYLTRANSFERASE; MAGNESIUM ION; MONOMER; OROTATE PHOSPHORIBOSYLTRANSFERASE; OROTIDINE 5' PHOSPHATE DECARBOXYLASE; PYRIMIDINE NUCLEOTIDE; PYROPHOSPHATE;

ARTICLE; BINDING SITE; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME STRUCTURE; ESCHERICHIA COLI; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; PYRIMIDINE SYNTHESIS; SALMONELLA TYPHIMURIUM; STEREOCHEMISTRY;

AMINO ACID SEQUENCE; BINDING SITES; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; DIPHOSPHATES; ESCHERICHIA COLI; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; OROTATE PHOSPHORIBOSYLTRANSFERASE; PHOSPHATES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SULFATES;

EID: 0029990345     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi952226y     Document Type: Article

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