1gla
STRUCTURE OF THE REGULATORY COMPLEX OF ESCHERICHIA COLI IIIGLC WITH GLYCEROL KINASE
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OverviewOverview
The phosphocarrier protein IIIGlc is an integral component of the, bacterial phosphotransferase (PTS) system. Unphosphorylated IIIGlc, inhibits non-PTS carbohydrate transport systems by binding to diverse, target proteins. The crystal structure at 2.6 A resolution of one of the, targets, glycerol kinase (GK), in complex with unphosphorylated IIIGlc, glycerol, and adenosine diphosphate was determined. GK contains a region, that is topologically identical to the adenosine triphosphate binding, domains of hexokinase, the 70-kD heat shock cognate, and actin. IIIGlc, binds far from the catalytic site of GK, indicating that long-range, conformational changes mediate the inhibition of GK by IIIGlc. GK and, IIIGlc are bound by hydrophobic and electrostatic interactions, with only, one hydrogen bond involving an uncharged group. The phosphorylation site, of IIIGlc, His90, is buried in a hydrophobic environment formed by the, active site region of IIIGlc and a 3(10) helix of GK, suggesting that, phosphorylation prevents IIIGlc binding to GK by directly disrupting, protein-protein interactions.
About this StructureAbout this Structure
1GLA is a Protein complex structure of sequences from Escherichia coli with GOL as ligand. Active as Protein-N(pi)-phosphohistidine--sugar phosphotransferase, with EC number 2.7.1.69 Full crystallographic information is available from OCA.
ReferenceReference
Structure of the regulatory complex of Escherichia coli IIIGlc with glycerol kinase., Hurley JH, Faber HR, Worthylake D, Meadow ND, Roseman S, Pettigrew DW, Remington SJ, Science. 1993 Jan 29;259(5095):673-7. PMID:8430315
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