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. 2023 Oct 30;89(11):e01106-23. doi: 10.1128/aem.01106-23

FIG 10.

FIG 10

The effects of S106C, I108F, and L285P mutations on the structure of ChPPK. (A) The overall structure of ChPPK. The lid domain, Walker A motif, and Walker B motif were indicated with grayish blue, turquoise, and pink, respectively. (B) Schematic diagram of the α6 helix with or without S106C and I108F mutations. The hydrogen bonding network in the α6 helix of the wild-type ChPPK (C) and ChPPK with S106C and I108F mutations (D). (E) A schematic diagram of the α18 helix with or without S106C and I108F mutations. The wild-type residues were indicated in yellow, and the mutated residues were indicated in blue in B, C, D, and E.