C-di-GMP hydrolysis by Pseudomonas aeruginosa HD-GYP phosphodiesterases: analysis of the reaction mechanism and novel roles for pGpG.
In biofilms, the bacterial community optimizes the strategies to sense the environment and to communicate from cell to cell. A key player in the development of a bacterial biofilm is the second messenger c-di-GMP, whose intracellular levels are modulated by the opposite activity of diguanylate cycla...
Main Authors: | Valentina Stelitano, Giorgio Giardina, Alessandro Paiardini, Nicoletta Castiglione, Francesca Cutruzzolà, Serena Rinaldo |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2013-01-01
|
Series: | PLoS ONE |
Online Access: | http://europepmc.org/articles/PMC3774798?pdf=render |
Similar Items
-
Investigating the allosteric regulation of YfiN from Pseudomonas aeruginosa: clues from the structure of the catalytic domain.
by: Giorgio Giardina, et al.
Published: (2013-01-01) -
The HD-GYP Domain, Cyclic Di-GMP Signaling, and Bacterial Virulence to Plants
by: J. Maxwell Dow, et al.
Published: (2006-12-01) -
The Structure of an Unconventional HD-GYP Protein from <italic toggle="yes">Bdellovibrio</italic> Reveals the Roles of Conserved Residues in this Class of Cyclic-di-GMP Phosphodiesterases
by: Andrew L. Lovering, et al.
Published: (2011-11-01) -
Crystal structure of an EAL domain in complex with reaction product 5'-pGpG.
by: Julien Robert-Paganin, et al.
Published: (2012-01-01) -
Induction of native c-di-GMP phosphodiesterases leads to dispersal of pseudomonas aeruginosa biofilms
by: Andersen, Jens Bo, et al.
Published: (2021)