High resolution structure of the phosphohistidine-activated form of Escherichia coli cofactor-dependent phosphoglycerate mutase

J Biol Chem. 2001 Feb 2;276(5):3247-53. doi: 10.1074/jbc.M007318200. Epub 2000 Oct 18.


The active conformation of the dimeric cofactor-dependent phosphoglycerate mutase (dPGM) from Escherichia coli has been elucidated by crystallographic methods to a resolution of 1.25 A (R-factor 0.121; R-free 0.168). The active site residue His(10), central in the catalytic mechanism of dPGM, is present as a phosphohistidine with occupancy of 0.28. The structural changes on histidine phosphorylation highlight various features that are significant in the catalytic mechanism. The C-terminal 10-residue tail, which is not observed in previous dPGM structures, is well ordered and interacts with residues implicated in substrate binding; the displacement of a loop adjacent to the active histidine brings previously overlooked residues into positions where they may directly influence catalysis. E. coli dPGM, like the mammalian dPGMs, is a dimer, whereas previous structural work has concentrated on monomeric and tetrameric yeast forms. We can now analyze the sequence differences that cause this variation of quaternary structure.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Escherichia coli / enzymology*
  • Histidine / metabolism
  • Models, Molecular
  • Molecular Sequence Data
  • Phosphoglycerate Mutase / chemistry*
  • Phosphoglycerate Mutase / metabolism
  • Phosphorylation
  • Protein Folding
  • Protein Structure, Quaternary
  • Sequence Homology, Amino Acid


  • Histidine
  • Phosphoglycerate Mutase

Associated data

  • PDB/1E58