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. 2003 Jan;59(Pt 1):73-6.
doi: 10.1107/s0907444902018929. Epub 2002 Dec 19.

Structure of Escherichia coli uridine phosphorylase at 2.0 A

F Temple Burling  1 , Ryan Kniewel, John A Buglino, Tanya Chadha, Andrew Beckwith, Christopher D Lima
Affiliations

Structure of Escherichia coli uridine phosphorylase at 2.0 A

F Temple Burling et al. Acta Crystallogr D Biol Crystallogr. 2003 Jan.

Abstract

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.

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