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PleD allosteric product inhibition

Allosteric product inhibition

PleD shows direct non-competitive feedback inibition with a K_i of about 1 μM. There are two allosteric sites, the I_p (R₃₅₉ and D₃₆₂ of a RxxD sequence motif and R₃₉₀), and the I_s (R₃₁₃) in the PleD GGDEF domain that are involved in product binding across to GGDEF domains (cross-linking).

Binding of two intercalated results in of the two GGDEF domains in the dimer and keeps the two active sites (with bound ) apart form each other.

References

Activated PleD structure 2v0n:

• Wassmann P, Chan C, Paul R, Beck A, Heerklotz H, Jenal U, Schirmer T. Structure of BeF3- -modified response regulator PleD: implications for diguanylate cyclase activation, catalysis, and feedback inhibition. Structure. 2007 Aug;15(8):915-27. PMID:17697997 doi:http://dx.doi.org/10.1016/j.str.2007.06.016