4K6O

X-ray structure uridine phosphorylase from Vibrio cholerae in complex with 6-methyluracil at 1.17 A resolution

Summary for 4K6O

• Entry DOI: 10.2210/pdb4k6o/pdb
• Descriptor: Uridine phosphorylase, CHLORIDE ION, 6-methylpyrimidine-2,4-diol, ... (10 entities in total)
• Functional Keywords: rossmann fold, transferase
• Biological source: Vibrio cholerae
• Total number of polymer chains: 6
• Total formula weight: 165468.33

Authors

Prokofev, I.I.,Lashkov, A.A.,Gabdoulkhakov, A.G.,Betzel, C.,Mikhailov, A.M. (deposition date: 2013-04-16, release date: 2014-05-07, Last modification date: 2023-11-08)

Primary citation

Prokofev, I.I.,Lashkov, A.A.,Gabdulkhakov, A.G.,Dontsova, M.V.,Seregina, T.A.,Mironov, A.S.,Betzel, C.,Mikhailov, A.M.
Crystallization and preliminary X-ray study of Vibrio cholerae uridine phosphorylase in complex with 6-methyluracil.
Acta Crystallogr.,Sect.F, 70:60-63, 2014

PubMed Abstract: Uridine phosphorylase catalyzes the phosphorolysis of ribonucleosides, with the nitrogenous base and ribose 1-phosphate as products. Additionally, it catalyzes the reverse reaction of the synthesis of ribonucleosides from ribose 1-phosphate and a nitrogenous base. However, the enzyme does not catalyze the synthesis of nucleosides when the substrate is a nitrogenous base substituted at the 6-position, such as 6-methyluracil (6-MU). In order to explain this fact, it is essential to investigate the three-dimensional structure of the complex of 6-MU with uridine phosphorylase. 6-MU is a pharmaceutical agent that improves tissue nutrition and enhances cell regeneration by normalization of nucleotide exchange in humans. 6-MU is used for the treatment of diseases of the gastrointestinal tract, including infectious diseases. Here, procedures to obtain the uridine phosphorylase from the pathogenic bacterium Vibrio cholerae (VchUPh), purification of this enzyme, crystallization of the complex of VchUPh with 6-MU, and X-ray data collection and preliminary X-ray analysis of the VchUPh-6-MU complex at atomic resolution are reported.

PubMed: 24419619
DOI: 10.1107/S2053230X13031877

Experimental method

X-RAY DIFFRACTION (1.17 Å)