1GPR

REFINED CRYSTAL STRUCTURE OF IIA DOMAIN OF THE GLUCOSE PERMEASE OF BACILLUS SUBTILIS AT 1.9 ANGSTROMS RESOLUTION

Summary for 1GPR

• Entry DOI: 10.2210/pdb1gpr/pdb
• Descriptor: GLUCOSE PERMEASE (2 entities in total)
• Functional Keywords: phosphotransferase
• Biological source: Bacillus subtilis
• Cellular location: Cell membrane; Multi-pass membrane protein: P20166
• Total number of polymer chains: 1
• Total formula weight: 17396.79

Authors

Liao, D.-I.,Herzberg, O. (deposition date: 1991-09-25, release date: 1993-10-31, Last modification date: 2024-02-07)

Primary citation

Herzberg, O.
An atomic model for protein-protein phosphoryl group transfer.
J.Biol.Chem., 267:24819-24823, 1992

PubMed Abstract: 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.

PubMed: 1447219

Experimental method

X-RAY DIFFRACTION (1.9 Å)