Structural plasticity and catalysis regulation of a thermosensor histidine kinase.

ABSTRACT: Temperature sensing is essential for the survival of living cells. A major challenge is to understand how a biological thermometer processes thermal information to optimize cellular functions. Using structural and biochemical approaches, we show that the thermosensitive histidine kinase, DesK, from Bacillus subtilis is cold-activated through specific interhelical rearrangements in its central four-helix bundle domain. As revealed by the crystal structures of DesK in different functional states, the plasticity of this helical domain influences the catalytic activities of the protein, either by modifying the mobility of the ATP-binding domains for autokinase activity or by modulating binding of the cognate response regulator to sustain the phosphotransferase and phosphatase activities. The s

SUBMITTER: Albanesi D 

PROVIDER: S-EPMC2738621 | biostudies-literature | 2009 Sep

REPOSITORIES: biostudies-literature