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 7
Binding of a divalent metal ion in the active-site cleft of PA1611REC. (a) Diagram of the surface electrostatic potential of PA1611REC. Negatively charged regions are colored red and positively charged regions blue, respectively. Divalent metal ion Mg²⁺ (shown as a light green sphere) is located in the negatively charged active-site cleft and interacts with Asp522, Asp565 and Arg567 (shown as sticks). (b) Spatial position of the residues and water molecules involved in the interactions with Mg²⁺. The six coordination positions of Mg²⁺ are indicated with yellow dashed lines, whereas the interactions between the residues and water molecules are indicated with cyan dashed lines. Oxygen atoms of Glu521, Asp522, Arg567 and Asp565 are shown as red sticks; water molecules are displayed as small blue spheres.

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