1gpr
From Proteopedia
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REFINED CRYSTAL STRUCTURE OF IIA DOMAIN OF THE GLUCOSE PERMEASE OF BACILLUS SUBTILIS AT 1.9 ANGSTROMS RESOLUTION
Overview
The high resolution crystal structures of two interacting proteins from, the phosphoenolpyruvate:sugar phosphotransferase system, the, histidine-containing phosphocarrier protein (HPr) and the IIA domain of, glucose permease (IIA(Glc)) from Bacillus subtilis, provide the basis for, modeling the transient binary complex formed during the phosphoryl group, transfer. The complementarity of the interacting surfaces implies that no, major conformational transition is required. The negatively charged, phosphoryl group is buried in the interface, suggesting a key role for, electrostatic interactions. It is proposed that the phosphoryl transfer is, triggered by a switch between two salt bridges involving Arg-17 of the, HPr. The first, prior to phosphoryl group transfer, is intramolecular, with the phosphorylated His-15. The second, during the transfer, is, intermolecular, with 2 aspartate residues associated with the active site, of IIA(Glc). Such alternating ion pairs may be mechanistically important, in other protein-protein phosphotransfer reactions.
About this Structure
1GPR is a Single protein structure of sequence from Bacillus subtilis. Active as Protein-N(pi)-phosphohistidine--sugar phosphotransferase, with EC number 2.7.1.69 Full crystallographic information is available from OCA.
Reference
An atomic model for protein-protein phosphoryl group transfer., Herzberg O, J Biol Chem. 1992 Dec 5;267(34):24819-23. PMID:1447219
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