Supplementary Materials

This PDF file includes:

  • Fig. S1. Biochemical analyses of the KdpDE interaction.
  • Fig. S2. Stability of phosphorylated KdpE at 37°C.
  • Fig. S3. In trans autophosphorylation of KdpD.
  • Fig. S4. The DBD interacts with the CA domain of KdpD and its promoter DNA through an overlapping surface.
  • Fig. S5. Enzymatic activities of the KdpD mutants.
  • Fig. S6. Mutations do not affect protein folding or enzymatic activities of KdpDE.
  • Fig. S7. CTT deletion impedes KdpDE-mediated signaling.
  • Fig. S8. Comparison of HK-RR complex structures.
  • Fig. S9. The RD adopts a canonical interface with the DHp domain in the KdpDE complex structure.
  • Fig. S10. The catalytic module of KdpD adopts a symmetric and open conformation.
  • Fig. S11. KdpE adopts a conformation similar to that of inactive OmpR-PhoR family members.
  • Table S1. Data collection and refinement statistics.

[Download PDF]