Document Detail


Crystallization and preliminary X-ray study of Vibrio cholerae uridine phosphorylase in complex with 6-methyluracil.
MedLine Citation:
PMID:  24419619     Owner:  NLM     Status:  In-Data-Review    
Abstract/OtherAbstract:
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.
Authors:
Igor I Prokofev; Alexander A Lashkov; Azat G Gabdulkhakov; Mariya V Dontsova; Tatyana A Seregina; Alexander S Mironov; Christian Betzel; Al'bert M Mikhailov
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Publication Detail:
Type:  Journal Article     Date:  2013-12-24
Journal Detail:
Title:  Acta crystallographica. Section F, Structural biology communications     Volume:  70     ISSN:  2053-230X     ISO Abbreviation:  -     Publication Date:  2014 Jan 
Date Detail:
Created Date:  2014-01-14     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101620319     Medline TA:  Acta Crystallogr Sect F Struct Biol Commun     Country:  United States    
Other Details:
Languages:  eng     Pagination:  60-3     Citation Subset:  IM    
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