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5'-NUCLEOTIDASE FROM E. COLI5'-NUCLEOTIDASE FROM E. COLI
Structural highlights
FunctionUSHA_ECOLI Degradation of external UDP-glucose to uridine monophosphate and glucose-1-phosphate, which can then be used by the cell. Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. X-ray structure of the Escherichia coli periplasmic 5'-nucleotidase containing a dimetal catalytic site.,Knofel T, Strater N Nat Struct Biol. 1999 May;6(5):448-53. PMID:10331872[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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