Structural highlights
Function
[UDP_ECOLI] 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.
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
The 2.0 A crystal structure has been determined for Escherichia coli uridine phosphorylase (UP), an essential enzyme in nucleotide biosynthesis that catalyzes the phosphorolytic cleavage of the C-N glycosidic bond of uridine to ribose-1-phosphate and uracil. The structure determination of two independent monomers in the asymmetric unit revealed the residue composition and atomic details of the apo configurations of each active site. The native hexameric UP enzyme was revealed by applying threefold crystallographic symmetry to the contents of the asymmetric unit. The 2.0 A model reveals a closer structural relationship to other nucleotide phosphorylase enzymes than was previously appreciated.
Structure of Escherichia coli uridine phosphorylase at 2.0 A.,Burling FT, Kniewel R, Buglino JA, Chadha T, Beckwith A, Lima CD Acta Crystallogr D Biol Crystallogr. 2003 Jan;59(Pt 1):73-6. Epub 2002 Dec, 19. PMID:12499542[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Burling FT, Kniewel R, Buglino JA, Chadha T, Beckwith A, Lima CD. Structure of Escherichia coli uridine phosphorylase at 2.0 A. Acta Crystallogr D Biol Crystallogr. 2003 Jan;59(Pt 1):73-6. Epub 2002 Dec, 19. PMID:12499542
