The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families

Nature Structural Biology

Volumn 3, Issue 1, 1996, Pages 74-86

  Tesmer, John J G ^a   Klem, Thomas J ^b   Deras, Michael L ^b   Davisson, V Jo ^b   Smith, Janet L ^a  

^a PURDUE UNIVERSITY   (United States)

^b PURDUE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; ARGININOSUCCINATE SYNTHASE; GUANOSINE PHOSPHATE; INORGANIC PYROPHOSPHATASE; NICOTINAMIDE ADENINE DINUCLEOTIDE; SYNTHETASE;

ARTICLE; BINDING SITE; CATALYSIS; CRYSTAL STRUCTURE; DIMERIZATION; HYDROLYSIS; PRIORITY JOURNAL; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; CARBON-NITROGEN LIGASES; CONSERVED SEQUENCE; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; LIGASES; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION;

EID: 0030024963     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb0196-74     Document Type: Article

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