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 8
Overall structure and interface of (a) the HptB–PA1611REC complex model and the complexes of (b) SLN1-R1/YPD1 and (c) AHK5_RD/AHP1. The ribbon diagrams illustrate (a) the docking model of the HptB–PA1611REC complex and the structures determined of (b) SLN1-R1/YPD1 and (c) AHK5_RD/AHP1 complexes. The molecules of HptB, PA1611REC-Mg²⁺, SLN1-R1, YPD1, AHK5_RD and AHP1 are colored wheat, green, blue, salmon, magenta and dark gray, respectively. The Mg²⁺ ion is shown as a yellow sphere. The interface of the complexes, analyzed using the PDBePISA web server, is shown in the surface presentation. The residues involved in the formation of hydrogen bonds or salt bridges are colored orange, whereas the residues contributing to the hydrophobic and van der Waals interactions are colored purple.

IUCrJ

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

ISSN: 2052-2525

https://doi.org/10.1107/S2052252520009665

BIOLOGY | MEDICINE

Open

access

Follow IUCrJ

Search IUCr Journals		doi		Advanced search
Author		volume	page