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.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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5'-Nucleotidase / chemistry*
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5'-Nucleotidase / metabolism
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Amino Acid Sequence
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Animals
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Aspartic Acid / chemistry
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Aspartic Acid / metabolism
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Binding Sites
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Catalysis
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Crystallization
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Crystallography, X-Ray
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Escherichia coli / enzymology*
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Histidine / chemistry
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Histidine / metabolism
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Humans
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Ligands
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Models, Molecular
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Molecular Sequence Data
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Phosphoric Monoester Hydrolases / chemistry
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Protein Conformation
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Protein Structure, Secondary
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Sequence Alignment
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Sequence Homology, Amino Acid
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Zinc / metabolism*
Substances
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Ligands
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Aspartic Acid
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Histidine
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Phosphoric Monoester Hydrolases
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5'-Nucleotidase
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Zinc