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- Title
Structural and mechanistic determinants of c-di-GMP signalling.
- Authors
Schirmer, Tilman; Jenal, Urs
- Abstract
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.
- Publication
Nature reviews. Microbiology, 2009, Vol 7, Issue 10, p724
- ISSN
1740-1534
- Publication type
Journal Article
- DOI
10.1038/nrmicro2203