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Nat Rev Microbiol. 2009 Oct;7(10):724-35. doi: 10.1038/nrmicro2203.

Structural and mechanistic determinants of c-di-GMP signalling.

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Biozentrum, University of Basel, Klingelbergstrasse 50, CH-4056 Basel, Switzerland.


Bis-(3'-5')-cyclic dimeric GMP (c-di-GMP) is a ubiquitous second messenger that regulates cell surface-associated traits in bacteria. Components of this regulatory network include GGDEF and EAL domain-containing proteins that determine the cellular concentrations of c-di-GMP by mediating its synthesis and degradation, respectively. Crystal structure analyses in combination with functional studies have revealed the catalytic mechanisms and regulatory principles involved. Downstream, c-di-GMP is recognized by PilZ domain-containing receptors that can undergo large-scale domain rearrangements on ligand binding. Here, we review recent data on the structure and functional properties of the protein families that are involved in c-di-GMP signalling and discuss the mechanistic implications.

[Indexed for MEDLINE]

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