Crystal structures of C4-dicarboxylate ligand complexes with sensor domains of histidine kinases DcuS and DctB.

ABSTRACT: Two-component signaling systems allow bacteria to adapt to changing environments. Typically, a chemical or other stimulus is detected by the periplasmic sensor domain of a transmembrane histidine kinase sensor, which in turn relays a signal through a phosphotransfer cascade to the cognate cytoplasmic response regulator. Such systems lead ultimately to changes in gene expression or cell motility. Mechanisms of ligand binding and signal transduction through the cell membrane in histidine kinases are not fully understood. In an effort to further understand such processes, we have solved the crystal structures of the periplasmic sensor domains of Escherichia coli DcuS and of Vibrio cholerae DctB in complex with the respective cognate ligands, malate and succinate. Both proteins are involved in

SUBMITTER: Cheung J 

PROVIDER: S-EPMC2573060 | biostudies-literature | 2008 Oct

REPOSITORIES: biostudies-literature