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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 59 73-6 (2003)
Cited: 7 times
EuropePMC logo PMID: 12499542

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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  2. Glycal formation in crystals of uridine phosphorylase. Paul D, O'Leary SE, Rajashankar K, Bu W, Toms A, Settembre EC, Sanders JM, Begley TP, Ealick SE. Biochemistry 49 3499-3509 (2010)
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Articles citing this publication (4)

  1. Implications of the structure of human uridine phosphorylase 1 on the development of novel inhibitors for improving the therapeutic window of fluoropyrimidine chemotherapy. Roosild TP, Castronovo S, Fabbiani M, Pizzorno G. BMC Struct Biol 9 14 (2009)
  2. A novel structural mechanism for redox regulation of uridine phosphorylase 2 activity. Roosild TP, Castronovo S, Villoso A, Ziemba A, Pizzorno G. J Struct Biol 176 229-237 (2011)
  3. Active site conformational dynamics in human uridine phosphorylase 1. Roosild TP, Castronovo S. PLoS One 5 e12741 (2010)
  4. 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 66 51-60 (2010)


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