Structural basis of Zn(II) induced metal detoxification and antibiotic resistance by histidine kinase CzcS in Pseudomonas aeruginosa
Fig 6
Proposed molecular mechanism of Zn(II) signal transduction in HK CzcS.
The two monomers in the CzcS functional dimer are shown in green and in cyan. When the Zn(II) binds to CzcS, the sensor domain will turn from monomer to dimer with the Zn(II) binding at the symmetrical N-terminal α-helices. The dimerization of sensor domain will drive the interactional rearrangement within the dimeric four-helical bundles in the transmembrane domain [47], and autophosphorylation is activated at the conserved histidine residues in the cytoplasmic kinase domain [48–51].