Protein folding modulates the swapped dimerization mechanism of methyl-accepting chemotaxis heme sensors.

ABSTRACT: The periplasmic sensor domains GSU0582 and GSU0935 are part of methyl accepting chemotaxis proteins in the bacterium Geobacter sulfurreducens. Both contain one c-type heme group and their crystal structures revealed that these domains form swapped dimers with a PAS fold formed from the two protein chains. The swapped dimerization of these sensors is related to the mechanism of signal transduction and the formation of the swapped dimer involves significant folding changes and conformational rearrangements within each monomeric component. However, the structural changes occurring during this process are poorly understood and lack a mechanistic framework. To address this issue, we have studied the folding and stability properties of two distinct heme-sensor PAS domains, using biophysical spec

SUBMITTER: Silva MA 

PROVIDER: S-EPMC3460858 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature