1e58
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E.COLI COFACTOR-DEPENDENT PHOSPHOGLYCERATE MUTASE
OverviewOverview
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 ... [(full description)]
About this StructureAbout this Structure
1E58 is a [Single protein] structure of sequence from [Escherichia coli] with SO4 and CL as [ligands]. The following page contains interesting information on the relation of 1E58 with [The Glycolytic Enzymes]. Active as [Phosphoglycerate mutase], with EC number [5.4.2.1]. Structure known Active Site: HIS. Full crystallographic information is available from [OCA].
ReferenceReference
High resolution structure of the phosphohistidine-activated form of Escherichia coli cofactor-dependent phosphoglycerate mutase., Bond CS, White MF, Hunter WN, J Biol Chem. 2001 Feb 2;276(5):3247-53. Epub 2000 Oct 18. PMID:11038361
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