Biological insights from structures of twocomponent proteins, Annu. Rev. Microbiol, vol.63, pp.133-154, 2009. ,
Receiver domain structure and function in response regulator proteins, Curr. Opin. Microbiol, vol.13, pp.142-149, 2010. ,
Molecular strategies for phosphorylationmediated regulation of response regulator activity, Curr. Opin. Microbiol, vol.13, pp.160-167, 2010. ,
Two-state allosteric behavior in a single-domain signaling protein, Science, vol.291, pp.2429-2433, 2001. ,
Structure of the Escherichia coli response regulator NarL, Biochemistry, vol.35, pp.11053-11061, 1996. ,
Effect of phosphorylation on the interdomain interaction of the response regulator, NarL. Biochemistry, vol.41, pp.15173-15180, 2002. ,
Regulation of response regulator autophosphorylation through interdomain contacts, J. Biol. Chem, vol.285, pp.32325-32335, 2010. ,
Probing the roles of the two different dimers mediated by the receiver domain of the response regulator PhoB, J. Mol. Biol, vol.389, pp.349-364, 2009. ,
Comprehensive analysis of OmpR phosphorylation, dimerization, and DNA binding supports a canonical model for activation, J. Mol. Biol, vol.425, pp.1612-1626, 2013. ,
Phosphorylationdependent conformational changes and domain rearrangements in Staphylococcus aureus VraR activation, Proc. Natl. Acad. Sci. U. S. A, vol.110, pp.8525-8530, 2013. ,
Crystal structure of the response regulator spr1814 from Streptococcus pneumoniae reveals unique interdomain contacts among NarL family proteins, Biochem. Biophys. Res. Commun, vol.434, pp.65-69, 2013. ,
Structural insight into partner specificity and phosphoryl transfer in two-component signal transduction, Cell, vol.139, pp.325-336, 2009. ,
Structural plasticity and catalysis regulation of a thermosensor histidine kinase, Proc. Natl. Acad. Sci. U. S. A, vol.106, pp.16185-16190, 2009. ,
Structural and enzymatic insights into the ATP binding and autophosphorylation mechanism of a sensor histidine kinase, J. Biol. Chem, vol.285, pp.24892-24903, 2010. ,
URL : https://hal.archives-ouvertes.fr/pasteur-00508936
Visualizing autophosphorylation in histidine kinases, Nat. Commun, vol.5, p.3258, 2014. ,
Segmental helical motions and dynamical asymmetry modulate histidine kinase autophosphorylation, PLoS Biol, vol.12, p.1001776, 2014. ,
Using structural information to change the phosphotransfer specificity of a twocomponent chemotaxis signalling complex, PLoS Biol, vol.8, p.1000306, 2010. ,
Solution structure of a complex of the histidine autokinase CheA with its substrate CheY, Biochemistry, vol.51, pp.3786-3798, 2012. ,
Structural basis of response regulator dephosphorylation by Rap phosphatases, PLoS Biol, vol.9, p.1000589, 2011. ,
A transient interaction between two phosphorelay proteins trapped in a crystal lattice reveals the mechanism of molecular recognition and phosphotransfer in signal transduction, Structure, vol.8, issue.00, p.174, 2000. ,
Structure and catalytic mechanism of the E. coli chemotaxis phosphatase CheZ, Nat. Struct. Biol, vol.9, pp.570-575, 2002. ,
Molecular basis of thermosensing: a two-component signal transduction thermometer in Bacillus subtilis, EMBO J, vol.20, pp.1681-1691, 2001. ,
Bacillus subtilis DesR functions as a phosphorylation-activated switch to control membrane lipid fluidity, J. Biol. Chem, vol.279, pp.39340-39347, 2004. ,
Oligomerization of Bacillus subtilis DesR is required for fine tuning regulation of membrane fluidity, Biochim. Biophys. Acta, vol.1790, pp.1238-1243, 2009. ,
Crystal structure of an activated response regulator bound to its target, Nat. Struct. Biol, vol.8, pp.52-56, 2001. ,
NarL dimerization? Suggestive evidence from a new crystal form, Biochemistry, vol.37, pp.3665-3676, 1998. ,
Conformational changes induced by phosphorylation of the FixJ receiver domain, Structure, vol.7, pp.1505-1515, 1999. ,
URL : https://hal.archives-ouvertes.fr/hal-00314286
Structure of a transiently phosphorylated switch in bacterial signal transduction, Nature, vol.402, pp.894-898, 1999. ,
Crystal structure of activated CheY. Comparison with other activated receiver domains, J. Biol. Chem, vol.276, pp.16425-16431, 2001. ,
Direct-coupling analysis of residue coevolution captures native contacts across many protein families, Proc. Natl. Acad. Sci. U. S. A, vol.108, pp.1293-1301, 2011. ,
URL : https://hal.archives-ouvertes.fr/hal-01589010
Identification of direct residue contacts in protein-protein interaction by message passing, Proc. Natl. Acad. Sci. U. S. A, vol.106, pp.67-72, 2009. ,
A link between dimerization and autophosphorylation of the response regulator PhoB, J. Biol. Chem, vol.288, pp.21755-21769, 2013. ,
Phosphate-binding tag, a new tool to visualize phosphorylated proteins, Mol. Cell. Proteomics, vol.5, pp.749-757, 2006. ,
Identical phosphatase mechanisms achieved through distinct modes of binding phosphoprotein substrate, Proc. Natl. Acad. Sci. U. S. A, vol.107, pp.1924-1929, 2010. ,
Rewiring the specificity of two-component signal transduction systems, Cell, vol.133, pp.1043-1054, 2008. ,
High-resolution NMR structure and backbone dynamics of the Bacillus subtilis response regulator, Spo0F: implications for phosphorylation and molecular recognition, Biochemistry, vol.36, pp.10015-10025, 1997. ,
A distinct meta-active conformation in the 1.1-A resolution structure of wild-type ApoCheY, J. Biol. Chem, vol.276, pp.28637-28640, 2001. ,
Three-dimensional solution structure of the N-terminal receiver domain of NTRC, Biochemistry, vol.34, pp.1413-1424, 1995. ,
Structural basis of a rationally rewired protein-protein interface critical to bacterial signaling, Structure, vol.21, pp.1636-1647, 2013. ,
Adaptive mutations that prevent crosstalk enable the expansion of paralogous signaling protein families, Cell, vol.150, pp.222-232, 2012. ,
Transient non-native hydrogen bonds promote activation of a signaling protein, Cell, vol.139, pp.1109-1118, 2009. ,
Crystal structures of the receiver domain of the response regulator PhoP from Escherichia coli in the absence and presence of the phosphoryl analog beryllofluoride, J. Bacteriol, vol.189, pp.5987-5995, 2007. ,
Molecular physiology of mammalian glucokinase, Cell. Mol. Life Sci, vol.66, pp.27-42, 2009. ,
Cooperativity in cellular biochemical processes: noiseenhanced sensitivity, fluctuating enzyme, bistability with nonlinear feedback, and other mechanisms for sigmoidal responses, Annu. Rev. Biophys, vol.41, pp.179-204, 2012. ,
FixL of Rhizobium meliloti enhances the transcriptional activity of a mutant FixJD54N protein by phosphorylation of an alternate residue, J. Bacteriol, vol.176, pp.1969-1976, 1994. ,
The acetate switch. Microbiol, Mol. Biol. Rev, vol.69, pp.12-50, 2005. ,
The intracellular concentration of acetyl phosphate in Escherichia coli is sufficient for direct phosphorylation of two-component response regulators, J. Bacteriol, vol.189, pp.5574-5581, 2007. ,
An atypical receiver domain controls the dynamic polar localization of the Myxococcus xanthus social motility protein FrzS, Mol. Microbiol, vol.65, pp.319-332, 2007. ,
Structure of an atypical orphan response regulator protein supports a new phosphorylationindependent regulatory mechanism, J. Biol. Chem, vol.282, pp.20667-20675, 2007. ,
Phosphorylation-independent activation of the atypical response regulator NblR, Microbiology, vol.154, pp.3002-3015, 2008. ,
Phosphorylation-independent activity of atypical response regulators of Helicobacter pylori, J. Bacteriol, vol.187, pp.3100-3109, 2005. ,
Autoregulation of antibiotic biosynthesis by binding of the end product to an atypical response regulator, Proc. Natl. Acad. Sci. U. S. A, vol.106, pp.8617-8622, 2009. ,
Allosteric regulation of histidine kinases by their cognate response regulator determines cell fate, Cell, vol.133, pp.452-461, 2008. ,
Phaser crystallographic software, J. Appl. Crystallogr, vol.40, pp.658-674, 2007. ,
Features and development of Coot, Acta Crystallogr. D Biol. Crystallogr, vol.66, pp.486-501, 2010. ,
,
Universally applicable methods for monitoring response regulator aspartate phosphorylation both in vitro and in vivo using phos-tag-based reagents, Anal. Biochem, vol.376, pp.73-82, 2008. ,