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 3
Overall structure of HptB. (a) Ribbon diagram illustrating the crystal packing in the native HptB crystal. There are six protein molecules in one asymmetric unit. (b) Diagram showing the structures are well superimposed among the six HptB protomers in the asymmetric unit. (c) Ribbon diagram illustrating the structural folding and secondary-structure elements of the HptB monomer. The helices are numbered sequentially α1 to α5 from the N-terminus to the C-terminus. The side-chain carbon and nitrogen atoms of the active-site histidine (His57) are shown as white and blue sticks, respectively. (d) Bottom view of the structure from (c). The side chain of His57 is highly exposed to solvent. The four-helix bundle core is composed of helices α2, α3, α4 and α5. (e) Stereoview of the HptB structure. Helix α1 forms a cap on top of the four-helix bundle.

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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