1LX7

Structure of E. coli uridine phosphorylase at 2.0A

Summary for 1LX7

• Entry DOI: 10.2210/pdb1lx7/pdb
• Related: 1k3f
• Descriptor: uridine phosphorylase (2 entities in total)
• Functional Keywords: structural genomics, udrpase, p12758, phosphorylase, nucleotide metabolism, psi, protein structure initiative, new york sgx research center for structural genomics, nysgxrc, transferase
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 55128.43

Authors

Burling, T.,Buglino, J.A.,Kniewel, R.,Chadna, T.,Beckwith, A.,Lima, C.D.,Burley, S.K.,New York SGX Research Center for Structural Genomics (NYSGXRC) (deposition date: 2002-06-04, release date: 2002-06-12, Last modification date: 2024-10-30)

Primary citation

Burling, F.T.,Kniewel, R.,Buglino, J.A.,Chadha, T.,Beckwith, A.,Lima, C.D.
Structure of Escherichia coli uridine phosphorylase at 2.0 A.
Acta Crystallogr.,Sect.D, 59:73-76, 2003

PubMed 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.

PubMed: 12499542
DOI: 10.1107/S0907444902018929

Experimental method

X-RAY DIFFRACTION (2 Å)