1K3F

Uridine Phosphorylase from E. coli, Refined in the Monoclinic Crystal Lattice

1K3F の概要

• エントリーDOI: 10.2210/pdb1k3f/pdb
• 分子名称: uridine phosphorylase (1 entity in total)
• 機能のキーワード: nucleoside phosphorylase, hexamer, transferase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm: P12758
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 163134.33

構造登録者

Morgunova, E.Yu.,Mikhailov, A.M.,Popov, A.N.,Blagova, E.V.,Smirnova, E.A.,Vainshtein, B.K.,Mao, C.,Armstrong, S.R.,Ealick, S.E.,Komissarov, A.A.,Linkova, E.V.,Burlakova, A.A.,Mironov, A.S.,Debabov, V.G. (登録日: 2001-10-02, 公開日: 2001-10-10, 最終更新日: 2024-04-03)

主引用文献

Morgunova, E.Yu.,Mikhailov, A.M.,Popov, A.N.,Blagova, E.V.,Smirnova, E.A.,Vainshtein, B.K.,Mao, C.,Armstrong, S.R.,Ealick, S.E.,Komissarov, A.A.,Linkova, E.V.,Burlakova, A.A.,Mironov, A.S.,Debabov, V.G.
Atomic structure at 2.5 A resolution of uridine phosphorylase from E. coli as refined in the monoclinic crystal lattice.
FEBS Lett., 367:183-187, 1995

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.

PubMed: 7796917
DOI: 10.1016/0014-5793(95)00489-V

実験手法

X-RAY DIFFRACTION (2.5 Å)