Role of Conformational Changes of Hexameric Bacterial Uridine Phosphorylases in Substrate Binding

Crystals of mutants of uridine phosphorylase from Shewanella oneidensis MR-1 at the active-site threonine residue were obtained, and the three-dimensional structures of the mutants were determined. It was shown that the loop 161–179 responsible for the nucleoside recognition is involved in stabiliza...

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Bibliographic Details
Published in:Crystallography reports 2021-09, Vol.66 (5), p.786-790
Main Authors: Polyakov, K. M., Mordkovich, N. N., Safonova, T. N., Antipov, A. N., Okorokova, N. A., Dorovatovskii, P. V., Veiko, V. P.
Format: Article
Language:English
Subjects:
Crystallography and Scattering Methods
Enzymes
Nucleosides
Phosphorylases
Physics
Physics and Astronomy
Structure of Macromolecular Compounds
Substrates
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Summary:Crystals of mutants of uridine phosphorylase from Shewanella oneidensis MR-1 at the active-site threonine residue were obtained, and the three-dimensional structures of the mutants were determined. It was shown that the loop 161–179 responsible for the nucleoside recognition is involved in stabilization of the hexameric structure of the protein and its disorder significantly facilitates the access of nucleoside to the enzyme active site. The role of conformational changes in the enzyme function is discussed.
ISSN:1063-7745
1562-689X
DOI:10.1134/S1063774521050199