Crystallization and preliminary X-ray study of Vibrio cholerae uridine phosphorylase in complex with 6-methyluracil
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 cataly...
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Published in | Acta crystallographica. Section F, Structural biology communications Vol. 70; no. 1; pp. 60 - 63 |
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Main Authors | , , , , , , , |
Format | Journal Article |
Language | English |
Published |
5 Abbey Square, Chester, Cheshire CH1 2HU, England
International Union of Crystallography
01.01.2014
Wiley Subscription Services, Inc |
Subjects | |
Online Access | Get full text |
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Summary: | 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. |
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Bibliography: | istex:AE9E9A4AB958FB580BD110C2E5DB6205E4FDA698 ArticleID:AYF2FW5433 ark:/67375/WNG-1RPJCKV7-1 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 2053-230X 2053-230X |
DOI: | 10.1107/S2053230X13031877 |