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 4
Hydrogen-bond linkages in the inter-helical regions of HptB. The diagrams illustrate the hydrogen bonds (yellow dashed lines) in the inter-helical regions between (a) helices α1 and α2; (b) helices α2 and α3; (c) helices α3 and α4; (d) helices α4 and α5. Carbon, nitrogen and oxygen atoms of the residues involved in the hydrogen-bond linkages are shown as white, blue and red sticks, respectively. Most interactions occur through main-chain atoms of residues. With the exception of Asp48 (at position −9 from the active-site histidine His57) and Pro91, the side chains of residues have been omitted for clarity of the main-chain interactions. The distances listed are the corresponding values averaged over the six molecules in the asymmetric unit. The conserved residues involved in the hydrogen-bond linkages are labeled with numbers in parentheses to indicate their positions from the active-site histidine His57.

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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