Atomic structure at 2.5 A resolution of uridine phosphorylase from E. coli as refined in the monoclinic crystal lattice.

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Citation

Morgunova EYu, Mikhailov AM, Popov AN, Blagova EV, Smirnova EA, Vainshtein BK, Mao C, Armstrong ShR, Ealick SE, Komissarov AA, et al.

Atomic structure at 2.5 A resolution of uridine phosphorylase from E. coli as refined in the monoclinic crystal lattice.

FEBS Lett. 1995 Jun 26;367(2):183-7.

PubMed ID
7796917 [ View in PubMed
]
Abstract

Uridine phosphorylase from E. coli (Upase) has been crystallized using vapor diffusion technique in a new monoclinic crystal form. The structure was determined by the molecular replacement method at 2.5 A resolution. The coordinates of the trigonal crystal form were used as a starting model and the refinement by the program XPLOR led to the R-factor of 18.6%. The amino acid fold of the protein was found to be the same as that in the trigonal crystals. The positions of flexible regions were refined. The conclusion about the involvement in the active site is in good agreement with the results of the biochemical experiments.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Uridine phosphorylaseP12758Details