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Acta Cryst. (2016). D72, 203-210
https://doi.org/10.1107/S2059798315024353
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Concerted action of two subunits of the functional dimer of Shewanella oneidensis MR-1 uridine phosphorylase derived from a comparison of the C212S mutant and the wild-type enzyme

T. N. Safonova, N. N. Mordkovich, V. P. Veiko, N. A. Okorokova, V. A. Manuvera, P. V. Dorovatovskii, V. O. Popov and K. M. Polyakov
The three-dimensional structure of the C212S mutant of uridine phosphorylase from S. oneidensis MR-1 was determined at 1.68 Å resolution. Binding of the substrate was shown to require the concerted action of two subunits of the functional dimer.
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