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Cyclic di-GMP signaling


Contents

Intro

Diguanylate cyclases

The condensation reaction 2 GTP -> c-di-GMP + 2 PPi is catalyzed by GGDEF domains that typically occur in combination with sensory or regulator domains. The structures of two diguanylate cyclases (PleD and WspR) have been determined, both being response regulators with a response regulator receiver (Rec) and a GGDEF output (effector) domain. Response regulators are activated through phosphorylation of a conserved aspartate by cognate histidine kinases.

PleD

   PleD catalysis

   PleD activation

   PleD allosteric product inhibition

WspR

C-di-GMP specific phosphodiesterases

Cleavage of one of the phosphodiester bonds is catalyzed by EAL and HD-GYP domains. Thereby, the cylic dinucleotide c-di-GMP is converted to the linear pGpG form.

Two structures of EAL domain proteins have been determined in complex with substrate c-di-GMP (YkuI 2w27 and BlrP1 3gg0) and are presented here.

C-di-GMP receptors with PilZ domain

References

Reviews:

  • Hengge R. Principles of c-di-GMP signalling in bacteria. Nat Rev Microbiol. 2009 Apr;7(4):263-73. PMID:19287449 doi:10.1038/nrmicro2109

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Tilman Schirmer

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