High Resolution Structure of the Phosphohistidine-activated Form of Escherichia coli Cofactor-dependent Phosphoglycerate Mutase

Charlie Bond, M.F. White, W.N. Hunter

Research output: Contribution to journalArticle

63 Citations (Scopus)

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 Angstrom (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.
Original languageEnglish
Pages (from-to)3247-3253
JournalJournal of Biological Chemistry
Volume276
Issue number5
DOIs
Publication statusPublished - 2001

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