Structure and function of the juxtamembrane GAF domain of potassium biosensor KdpD.

ABSTRACT: KdpD/KdpE two-component signaling system regulates expression of a high affinity potassium transporter responsible for potassium homeostasis. The C-terminal module of KdpD consists of a GAF domain linked to a histidine kinase domain. Whereas certain GAF domains act as regulators by binding cyclic nucleotides, the role of the juxtamembrane GAF domain in KdpD is unknown. We report the high-resolution crystal structure of KdpD GAF domain (KdpD^G ) consisting of five α-helices, four β-sheets and two large loops. KdpD^G forms a symmetry-related dimer, wherein parallelly arranged monomers contribute to a four-helix bundle at the dimer-interface, SAXS analysis of KdpD C-terminal module reveals an elongated structure that is a dimer in solution. Substitution of conserved residu

SUBMITTER: Kumar S 

PROVIDER: S-EPMC7454560 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature