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 5
Structural features around the active-site histidine (His57) of HptB. The diagram shows the hydrogen-bond linkage (yellow dashed line) between Lys60 and Glu79 near the active-site histidine (His57) and the spatial position of the highly conserved glycine residue (Gly61) at position +4 from His57. The indicated distance is a value averaged over six molecules in the asymmetric unit. Carbon, nitrogen and oxygen atoms of His57, Lys60, Gly61 and Glu79 are shown as white, blue and red sticks, respectively.

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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