Structural highlights
Function
[UDP_SALTY] Catalyzes the reversible phosphorylytic cleavage of uridine and deoxyuridine to uracil and ribose- or deoxyribose-1-phosphate. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis (By similarity).
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 PubMed
Uridine nucleoside phosphorylase is an important drug target for the development of anti-infective and antitumour agents. The X-ray crystal structure of Salmonella typhimurium uridine nucleoside phosphorylase (StUPh) complexed with its inhibitor 2,2'-anhydrouridine, phosphate and potassium ions has been solved and refined at 1.86 A resolution (R(cryst) = 17.6%, R(free) = 20.6%). The complex of human uridine phosphorylase I (HUPhI) with 2,2'-anhydrouridine was modelled using a computational approach. The model allowed the identification of atomic groups in 2,2'-anhydrouridine that might improve the interaction of future inhibitors with StUPh and HUPhI.
The X-ray structure of Salmonella typhimurium uridine nucleoside phosphorylase complexed with 2,2'-anhydrouridine, phosphate and potassium ions at 1.86 A resolution.,Lashkov AA, Zhukhlistova NE, Gabdoulkhakov AH, Shtil AA, Efremov RG, Betzel C, Mikhailov AM Acta Crystallogr D Biol Crystallogr. 2010 Jan;66(Pt 1):51-60. Epub 2009, Dec 21. PMID:20057049[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lashkov AA, Zhukhlistova NE, Gabdoulkhakov AH, Shtil AA, Efremov RG, Betzel C, Mikhailov AM. The X-ray structure of Salmonella typhimurium uridine nucleoside phosphorylase complexed with 2,2'-anhydrouridine, phosphate and potassium ions at 1.86 A resolution. Acta Crystallogr D Biol Crystallogr. 2010 Jan;66(Pt 1):51-60. Epub 2009, Dec 21. PMID:20057049 doi:10.1107/S0907444909044175
