1sj9
Crystal structure of the uridine phosphorylase from Salmonella typhimurium at 2.5A resolution
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OverviewOverview
Uridine phosphorylase (UPh) catalyzes the phosphorolytic cleavage of the, C-N glycosidic bond of uridine to ribose 1-phosphate and uracil in the, pyrimidine-salvage pathway. The crystal structure of the Salmonella, typhimurium uridine phosphorylase (StUPh) has been determined at 2.5 A, resolution and refined to an R factor of 22.1% and an Rfree of 27.9%. The, hexameric StUPh displays 32 point-group symmetry and utilizes both twofold, and threefold non-crystallographic axes. A phosphate is bound at the, active site and forms hydrogen bonds to Arg91, Arg30, Thr94 and Gly26 of, one monomer and Arg48 of an adjacent monomer. The hexameric StUPh model, reveals a close structural relationship to Escherichia coli uridine, phosphorylase (EcUPh).
About this StructureAbout this Structure
1SJ9 is a Single protein structure of sequence from Salmonella typhimurium with PO4 as ligand. Active as Uridine phosphorylase, with EC number 2.4.2.3 Full crystallographic information is available from OCA.
ReferenceReference
Preliminary investigation of the three-dimensional structure of Salmonella typhimurium uridine phosphorylase in the crystalline state., Dontsova MV, Gabdoulkhakov AG, Molchan OK, Lashkov AA, Garber MB, Mironov AS, Zhukhlistova NE, Morgunova EY, Voelter W, Betzel C, Zhang Y, Ealick SE, Mikhailov AM, Acta Crystallograph Sect F Struct Biol Cryst Commun. 2005 Apr 1;61(Pt, 4):337-40. Epub 2005 Mar 24. PMID:16511035
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