PMID:10331872

Citation	Knöfel, T and Sträter, N (1999) X-ray structure of the Escherichia coli periplasmic 5'-nucleotidase containing a dimetal catalytic site. Nat. Struct. Biol. 6:448-53
Abstract	The crystal structure of 5'-nucleotidase (5'-NT) from E. coli, also known as UDP-sugar hydrolase, has been determined at 1.7 A resolution. Two zinc ions are present in the active site, which is located in a cleft between two domains. The dimetal center and a catalytic Asp-His dyad are the main players in the catalytic mechanism. Structure-based sequence comparisons show that the structure also provides a model for animal 5'-NTs, which together with other ectonucleotidases terminate the action of nucleotides as extracellular signaling substances in the nervous system.
Links	PubMed Online version:10.1038/8253
Keywords	5'-Nucleotidase/chemistry; 5'-Nucleotidase/metabolism; Amino Acid Sequence; Animals; Aspartic Acid/chemistry; Aspartic Acid/metabolism; Binding Sites; Catalysis; Crystallization; Crystallography, X-Ray; Escherichia coli/enzymology; Histidine/chemistry; Histidine/metabolism; Humans; Ligands; Models, Molecular; Molecular Sequence Data; Phosphoric Monoester Hydrolases/chemistry; Protein Conformation; Protein Structure, Secondary; Sequence Alignment; Sequence Homology, Amino Acid; Zinc/metabolism
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