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Structural and mechanistic determinants of c-di-GMP signalling

Schirmer, Tilman and Jenal, Urs. (2009) Structural and mechanistic determinants of c-di-GMP signalling. Nature Reviews Microbiology, Vol. 7. pp. 724-735.

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Official URL: http://edoc.unibas.ch/dok/A5258229

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Abstract

Bis-(3'-5' -cyclic dimeric GMP (c-di-GMP) is a ubiquito us second messenger that regulates cell surface-associated traits in bacteria. Components of this regulatory network include GGDEF and EAL domain-containing proteins that det ermine the cellular concentrations of c-di-GMP by mediatin g its synthesis and degradation, respectively. Crystal str ucture analyses in combination with functional studies have revealed the catalytic mechanisms and regulatory princip les involved. Downstream, c-di-GMP is recognized by PilZ d omain-containing receptors that can undergo large-scale do main rearrangements on ligand binding. Here, we review rec ent data on the structure and functional properties of the protein families that are involved in c-di-GMP signalling and discuss the mechanistic implications.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Schirmer)
UniBasel Contributors:Jenal, Urs and Schirmer, Tilman
Item Type:Article, refereed
Article Subtype:Research Article
Bibsysno:Link to catalogue
Publisher:Nature Publishing Group
ISSN:1740-1526
e-ISSN:1740-1534
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:13 Oct 2017 08:02
Deposited On:22 Mar 2012 13:28

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