Structural basis of KdpD histidine kinase binding to the second messenger c-di-AMP.

ABSTRACT: The KdpDE two-component system regulates potassium homeostasis and virulence in various bacterial species. The KdpD histidine kinases (HK) of this system contain a universal stress protein (USP) domain which binds to the second messenger cyclic-di-adenosine monophosphate (c-di-AMP) for regulating transcriptional output from this two-component system in Firmicutes such as Staphylococcus aureus. However, the structural basis of c-di-AMP specificity within the KdpD-USP domain is not well understood. Here, we resolved a 2.3 Å crystal structure of the S. aureus KdpD-USP domain (USP_Sa) complexed with c-di-AMP. Binding affinity analyses of USP_Sa mutants targeting the observed USP_Sa:c-di-AMP structural interface enabled the identification of the sequence residues t

SUBMITTER: Dutta A 

PROVIDER: S-EPMC8214093 | biostudies-literature | 2021 Jan-Jun

REPOSITORIES: biostudies-literature