Structural and enzymatic insights into the ATP binding and autophosphorylation mechanism of a sensor histidine kinase.

ABSTRACT: DesK is a sensor histidine kinase (HK) that allows Bacillus subtilis to respond to cold shock, triggering the adaptation of membrane fluidity via transcriptional control of a fatty acid desaturase. It belongs to the HK family HPK7, which includes the nitrogen metabolism regulators NarX/Q and the antibiotic sensor LiaS among other important sensor kinases. Structural information on different HK families is still scarce and several questions remain, particularly concerning the molecular features that determine HK specificity during its catalytic autophosphorylation and subsequent response-regulator phosphotransfer reactions. To analyze the ATP-binding features of HPK7 HKs and dissect their mechanism of autophosphorylation at the molecular level, we have studied DesK in complex with ATP using

SUBMITTER: Trajtenberg F 

PROVIDER: S-EPMC2915725 | biostudies-literature | 2010 Aug

REPOSITORIES: biostudies-literature