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

Morgunova EYu; A M Mikhailov; A N Popov; E V Blagova; E A Smirnova; B K Vainshtein; C Mao; Sh R Armstrong; S E Ealick; A A Komissarov

doi:10.1016/0014-5793(95)00489-v

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. doi: 10.1016/0014-5793(95)00489-v.

Authors

Morgunova EYu¹, A M Mikhailov, A N Popov, E V Blagova, E A Smirnova, B K Vainshtein, C Mao, Sh R Armstrong, S E Ealick, A A Komissarov, et al.

Affiliation

¹ Institute of Crystallography of Russian Academy of Sciences, Moscow.

PMID: 7796917
DOI: 10.1016/0014-5793(95)00489-v

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.

Publication types

Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

MeSH terms

Amino Acid Sequence
Binding Sites
Crystallography, X-Ray
Escherichia coli / enzymology*
Hydrogen Bonding
Models, Molecular
Molecular Sequence Data
Protein Conformation
Protein Structure, Secondary
Uridine Phosphorylase / chemistry*

Substances

Uridine Phosphorylase

Grants and funding

GM48874/GM/NIGMS NIH HHS/United States