Structural insights into the histidine-containing phospho­transfer protein and receiver domain of sensor histidine kinase suggest a complex model in the two-component regulatory system in Pseudomonas aeruginosa

Chen, S.-K.; Guan, H.-H.; Wu, P.-H.; Lin, L.-T.; Wu, M.-C.; Chang, H.-Y.; Chen, N.-C.; Lin, C.-C.; Chuankhayan, P.; Huang, Y.-C.; Lin, P.-J.; Chen, C.-J.

doi:10.1107/S2052252520009665

Figure 1
Schematic diagram of the phosphorelay in HptB-mediated hybrid TCS. The P. aeruginosa gene index numbers of the orphan sensors and the response regulator are listed in parentheses. Blue arrows indicate the phosphoryl transfer in the pathway. The phosphoryl group is presented with an encircled P. After activation with environmental stimuli, sensor histidine kinases (PA1611, PA1976, PA2824 and PA4856) autophosphorylate and transfer the phosphoryl group specifically to HptB, which in turn relays the signal to response regulator PA3346. The phosphorylation regulates the Ser/Thr phosphatase activity of PA3346, resulting in increased phosphatase activity and dephosphorylation of the anti-sigma antagonist PA3347 (indicated with a red arrow). The phosphorylation/dephosphorylation status might modulate the binding activity of PA3347 to other factor(s) and lead to the regulation of genes associated with swarming activity and biofilm formation.

IUCrJ

Volume 7| Part 5| September 2020| Pages 934-948

ISSN: 2052-2525

https://doi.org/10.1107/S2052252520009665

BIOLOGY | MEDICINE

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