1drk
|
PROBING PROTEIN-PROTEIN INTERACTIONS: THE RIBOSE-BINDING PROTEIN IN BACTERIAL TRANSPORT AND CHEMOTAXIS
OverviewOverview
A number of mutations at Gly134 of the periplasmic ribose-binding protein, of Escherichia coli were examined by a combined biochemical and structural, approach. Different mutations gave rise to different patterns of effects, on the chemotaxis and transport functions. The smallest residue (alanine), had the least effect on transport, whereas large hydrophobic residues had, the smallest effect on chemotaxis. Comparison of the x-ray crystal, structure of the G134R mutant protein (2.5-A resolution) to that of the, wild type (1.6-A resolution) showed that the basic structure of the, protein was unaltered. The loss of chemotaxis and transport functions in, this and similar mutant proteins must therefore be caused by relatively, simple surface effects, which include a change in local main chain, conformation. The loss of chemotaxis and transport functions resulting, from the introduction of an alanine residue at position 134 was suppressed, by an additional isoleucine to threonine mutation at residue 132. An x-ray, structure of the I132T/G134A double mutant protein (2.2-A resolution), showed that the changes in local structure were accompanied by a diffuse, pattern of structural changes in the surrounding region, implying that the, suppression derives from a combination of sources.
About this StructureAbout this Structure
1DRK is a Single protein structure of sequence from Escherichia coli with RIP as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Probing protein-protein interactions. The ribose-binding protein in bacterial transport and chemotaxis., Bjorkman AJ, Binnie RA, Zhang H, Cole LB, Hermodson MA, Mowbray SL, J Biol Chem. 1994 Dec 2;269(48):30206-11. PMID:7982928
Page seeded by OCA on Tue Nov 20 13:31:41 2007