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

FEBS Lett. 1999 Sep 17;458(2):93-6. doi: 10.1016/s0014-5793(99)01103-5.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 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

Substances

  • Peptide Fragments
  • Aspartic Acid
  • Manganese
  • Phosphoenolpyruvate
  • Pyruvate Kinase
  • Phosphoenolpyruvate Carboxylase

Associated data

  • PDB/1QB4