Plausible phosphoenolpyruvate binding site revealed by 2.6 Å structure of Mn2+‐bound phosphoenolpyruvate carboxylase from Escherichia coli

FEBS Letters

Izui, Katsura²  Shirakata, Shunsuke³  Kai, Yasushi³  Matsumura, Hiroyoshi³  Terada, Mika³  Yoshinaga, Takeo¹  Inoue, Tsuyoshi³ 

[1] Department of Public Health, Graduate School of Medicine, Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan;Division of Integrated Life Science, Graduate School of Biostudies, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan;Department of Materials Chemistry, Graduate School of Engineering, Osaka University, Suita, Osaka 565-0871, Japan

关键词: Phosphoenolpyruvate carboxylase;    Crystal structure;    Mn2+-bound form;    Phosphoenolpyruvate binding site;    PEPC;    phosphoenolpyruvate carboxylase;    PEP;    phosphoenolpyruvate;    OAA;    oxaloacetate;    CAM;    crassulacean acid metabolism;    CoASc;    acetyl coenzyme A;    PEG;    polyethylene glycol;    PK;    pyruvate kinase;    PPDK;    pyruvate phosphate dikinase;    DCDP;    3;    3-dichloro-2-dihydroxyphosphinoylmethyl-2-propenoate;   

DOI  :  10.1016/S0014-5793(99)01103-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We have determined the crystal structure of Mn²⁺-bound Escherichia coli phosphoenolpyruvate carboxylase (PEPC) using X-ray diffraction at 2.6 Å resolution, and specified the location of enzyme-bound Mn²⁺, which is essential for catalytic activity. The electron density map reveals that Mn²⁺ is bound to the side chain oxygens of Glu-506 and Asp-543, and located at the top of the α/β barrel in PEPC. The coordination sphere of Mn²⁺ observed in E. coli PEPC is similar to that of Mn²⁺ found in the pyruvate kinase structure. The model study of Mn²⁺-bound PEPC complexed with phosphoenolpyruvate (PEP) reveals that the side chains of Arg-396, Arg-581 and Arg-713 could interact with PEP.

【 授权许可】

Unknown