Comparative Study
doi: 10.1038/8253.
X-ray structure of the Escherichia coli periplasmic 5'-nucleotidase containing a dimetal catalytic site
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- PMID: 10331872
- DOI: 10.1038/8253
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Comparative Study
X-ray structure of the Escherichia coli periplasmic 5'-nucleotidase containing a dimetal catalytic site
Nat Struct Biol.
1999 May.
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.
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