Results 11 to 20 of about 104,269 (134)

The structure of an unconventional HD-GYP protein from Bdellovibrio reveals the roles of conserved residues in this class of cyclic-di-GMP phosphodiesterases. [PDF]

mBio, 2011
ABSTRACT Cyclic-di-GMP is a near-ubiquitous bacterial second messenger that is important in localized signal transmission during the control of various processes, including virulence and switching between planktonic and biofilm-based lifestyles.
Lovering AL, Capeness MJ, Lambert C, Hobley L, Sockett RE.   +4 more
europepmc   +6 more sources

Structural basis of functional diversification of the HD-GYP domain revealed by the Pseudomonas aeruginosa PA4781 protein, which displays an unselective bimetallic binding site. [PDF]

J Bacteriol, 2015
ABSTRACT The intracellular level of the bacterial secondary messenger cyclic di-3′,5′-GMP (c-di-GMP) is determined by a balance between its biosynthesis and degradation, the latter achieved via dedicated phosphodiesterases (PDEs) bearing a characteristic EAL or HD-GYP domain. We here report the crystal structure of PA4781, one of
Rinaldo S, Paiardini A, Stelitano V, Brunotti P, Cervoni L, Fernicola S, Protano C, Vitali M, Cutruzzolà F, Giardina G.   +9 more
europepmc   +5 more sources

Crystal structure of an HD-GYP domain cyclic-di-GMP phosphodiesterase reveals an enzyme with a novel trinuclear catalytic iron centre. [PDF]

Mol Microbiol, 2014
SummaryBis‐(3′,5′) cyclic di‐guanylate (c‐di‐GMP) is a key bacterial second messenger that is implicated in the regulation of many crucial processes that include biofilm formation, motility and virulence. Cellular levels of c‐di‐GMP are controlled through synthesis by GGDEF domain diguanylate cyclases and degradation by two classes of phosphodiesterase
Bellini D, Caly DL, McCarthy Y, Bumann M, An SQ, Dow JM, Ryan RP, Walsh MA.   +7 more
europepmc   +9 more sources

Gas-Selective Catalytic Regulation by a Newly Identified Globin-Coupled Sensor Phosphodiesterase Containing an HD-GYP Domain from the Human Pathogen Vibrio fluvialis. [PDF]

Biochemistry
Globin-coupled sensors constitute an important family of heme-based gas sensors, an emerging class of heme proteins. In this study, we have identified and characterized a globin-coupled sensor phosphodiesterase containing an HD-GYP domain (GCS-HD-GYP) from the human pathogen Vibrio fluvialis, which is an emerging foodborne pathogen of increasing public
Kitanishi K, Aoyama N, Shimonaka M.
europepmc   +4 more sources

Cell-cell signal-dependent dynamic interactions between HD-GYP and GGDEF domain proteins mediate virulence in Xanthomonas campestris. [PDF]

Proc Natl Acad Sci U S A, 2010
RpfG is a paradigm for a class of widespread bacterial two-component regulators with a CheY-like receiver domain attached to a histidine-aspartic acid-glycine-tyrosine-proline (HD-GYP) cyclic di-GMP phosphodiesterase domain. In the plant pathogen Xanthomonas campestris pv.
Ryan RP, McCarthy Y, Andrade M, Farah CS, Armitage JP, Dow JM.   +5 more
europepmc   +7 more sources

C-di-GMP hydrolysis by Pseudomonas aeruginosa HD-GYP phosphodiesterases: analysis of the reaction mechanism and novel roles for pGpG. [PDF]

PLoS One, 2013
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 cyclases and phosphodiesterases.
Stelitano V, Giardina G, Paiardini A, Castiglione N, Cutruzzolà F, Rinaldo S.   +5 more
europepmc   +8 more sources

The HD-GYP Domain, Cyclic Di-GMP Signaling, and Bacterial Virulence to Plants [PDF]

Molecular Plant-Microbe Interactions®, 2006
Cyclic di-GMP is an almost ubiquitous second messenger in bacteria that was first described as an allosteric activator of cellulose synthase but is now known to regulate a range of functions, including virulence in human and animal pathogens. Two protein domains, GGDEF and EAL, are implicated in the synthesis and degradation, respectively, of cyclic ...
Dow, J. Maxwell, Fouhy, Yvonne, Lucey, Jean F., Ryan, Robert P.   +3 more
openaire   +5 more sources

Intermolecular interactions between HD-GYP and GGDEF domain proteins mediate virulence-related signal transduction inXanthomonas campestris [PDF]

Virulence, 2010
In the plant pathogen Xanthomonas campestris pv. campestris (Xcc) a two component system comprising RpfG and the complex sensor kinase RpfC is implicated in sensing and responding to the cell-cell signaling molecule DSF to positively regulate the synthesis of virulence factors such as extracellular enzymes, biofilm structure and motility. RpfG is a two-
Ryan, Robert P., Dow, J. Maxwell
openaire   +4 more sources

Dynamic complex formation between HD-GYP, GGDEF and PilZ domain proteins regulates motility in Xanthomonas campestris. [PDF]

Molecular microbiology, 2013
RpfG is a member of a class of wide spread bacterial two-component regulators with an HD-GYP cyclic di-GMP phosphodiesterase domain. In the plant pathogen Xanthomonas campestris, RpfG together with the sensor kinase RpfC regulates multiple factors as a response to the cell-to-cell Diffusible Signalling Factor (DSF).
Ryan, R, McCarthy, Y, Kiely, P, O'Connor, R, Farah, C, Armitage, J, Dow, J   +6 more
core   +5 more sources

Formation of a complex between HD-GYP, GGDEF and PilZ domain proteins regulates motility in Xanthomonas campestris

Microbiology Research, 2018
RpfG is a member of a class of wide spread bacterial two-component regulators with an HD-GYP cyclic di-GMP phosphodiesterase domain. In the plant pathogen Xanthomonas campestris pv. campestris (Xcc), RpfG together with the sensor kinase RpfC regulates the synthesis of a range of virulence factors as a response to the cell-cell Diffusible Signaling ...
Shi-qi An, Ji-liang Tang
openaire   +3 more sources