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

FEBS Letters

Popov, A.N.¹  Debabov, V.G.³  Blagova, E.V.¹  Mao, Ch.²  Armstrong, Sh.R.²  Burlakova, A.A.³  Mironov, A.S.³  Linkova, E.V.³  Morgunova, E.Yu.¹  Mikhailov, A.M.¹  Smirnova, E.A.¹  Vainshtein, B.K.¹  Komissarov, A.A.³  Ealick, S.E.² 

[1] Institute of Crystallography of Russian Academy of Sciences, Leninsky Prospect 59, Moscow 117333, Russian Federation;Section of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, New York 14853, USA;State Scientific Centre of Russian GNIIGENETIKA, 1st Dorozhny 1, Moscow 113545, Russian Federation

关键词: Uridine phosphorylase;    E. coli;    X-ray structure;   

DOI  :  10.1016/0014-5793(95)00489-V

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 Å 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.

【 授权许可】

Unknown