PMID:10481043

Citation	Matsumura, H, Terada, M, Shirakata, S, Inoue, T, Yoshinaga, T, Izui, K and Kai, Y (1999) Plausible phosphoenolpyruvate binding site revealed by 2.6 A structure of Mn2+-bound phosphoenolpyruvate carboxylase from Escherichia coli. FEBS Lett. 458:93-6
Abstract	We have determined the crystal structure of Mn2+-bound Escherichia coli phosphoenolpyruvate carboxylase (PEPC) using X-ray diffraction at 2.6 A 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 alpha/beta 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.
Links	PubMed
Keywords	Animals; Aspartic Acid/chemistry; Binding Sites; Catalysis; Computer Simulation; Crystallography, X-Ray; Escherichia coli/enzymology; Manganese/chemistry; Manganese/metabolism; Models, Molecular; Peptide Fragments/chemistry; Phosphoenolpyruvate/chemistry; Phosphoenolpyruvate/metabolism; Phosphoenolpyruvate Carboxylase/chemistry; Phosphoenolpyruvate Carboxylase/metabolism; Protein Structure, Secondary; Pyruvate Kinase/chemistry; Rabbits; Sequence Homology, Amino Acid
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