User:Tilman Schirmer/Sandbox 213

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PleD allosteric product inhibition

Allosteric product inhibition

activated (BeF3- modified; 2v0n

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PleD shows direct non-competitive feedback inibition with a Ki of about 1 μM. There are two allosteric sites, the ''primary'' inhibition site Ip (R359 and D362 of a RxxD sequence motif and R390), and the "secondary'' inhibition site Is (R313) in the PleD GGDEF domain that are involved in product binding across to GGDEF domains (cross-linking).

Binding of two intercalated (c-di-GMP)2 dimers results in cross-linking of the two GGDEF domains in the dimer and keeps the two active sites (with bound substrate analog) apart form each other.



References

Activated PleD structure 2v0n:

  1. 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:https://dx.doi.org/10.1016/j.str.2007.06.016

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Tilman Schirmer

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