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1gla

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(New page: 200px<br /><applet load="1gla" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gla, resolution 2.6&Aring;" /> '''STRUCTURE OF THE REGU...)
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Revision as of 14:01, 20 November 2007


1gla, resolution 2.6Å

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STRUCTURE OF THE REGULATORY COMPLEX OF ESCHERICHIA COLI IIIGLC WITH GLYCEROL KINASE

Overview

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 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.

Reference

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

Page seeded by OCA on Tue Nov 20 16:08:23 2007

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