1E58

E.coli cofactor-dependent phosphoglycerate mutase

Summary for 1E58

• Entry DOI: 10.2210/pdb1e58/pdb
• Related: 1E59
• Descriptor: PHOSPHOGLYCERATE MUTASE, SULFATE ION, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: phosphohistidine, glycolysis and gluconeogenesis, phosphoglycerate mutase, isomerase
• Biological source: ESCHERICHIA COLI
• Total number of polymer chains: 1
• Total formula weight: 28771.74

Authors

Bond, C.S.,Hunter, W.N. (deposition date: 2000-07-19, release date: 2001-03-20, Last modification date: 2019-05-22)

Primary citation

Bond, C.S.,White, M.F.,Hunter, W.N.
High Resolution Structure of the Phosphohistidine-Activated Form of Escherichia Coli Cofactor-Dependent Phosphoglycerate Mutase.
J.Biol.Chem., 276:3247-, 2001

PubMed Abstract: 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.

PubMed: 11038361
DOI: 10.1074/JBC.M007318200

Experimental method

X-RAY DIFFRACTION (1.25 Å)