The Solvation of the E. coli CheY Phosphorylation Site Mapped by XFMS

The Escherichia coli CheY protein belongs to a large bacterial response regulator superfamily. X-ray hydroxy radical foot-printing with mass spectroscopy (XFMS) has shown that allosteric activation of CheY by its motor target triggers a concerted internalization of aromatic sidechains. We reanalyzed...

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Bibliographic Details
Published in:International journal of molecular sciences 2022-10, Vol.23 (21), p.12771
Main Authors: Hamid, Maham, Khalid, Muhammad Farhan, Chaudhary, Safee Ullah, Khan, Shahid
Format: Article
Language:English
Subjects:
Algorithms
Allosteric properties
Biochemistry & Molecular Biology
Bioinformatics
Chemistry
Chemotaxis
CheY protein
Dynamic structural analysis
E coli
Hydrogen
Hydrogen bonds
Hydrophobicity
Internalization
Mass spectroscopy
MATLAB toolbox
Oxidation
Phosphorylation
protection factor (PF)
protein phosphorylation
Proteins
Residues
Signal transduction
Solvation
solvent accessible surface area (SASA)
Solvents
Spectrum analysis
structured water
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Summary:The Escherichia coli CheY protein belongs to a large bacterial response regulator superfamily. X-ray hydroxy radical foot-printing with mass spectroscopy (XFMS) has shown that allosteric activation of CheY by its motor target triggers a concerted internalization of aromatic sidechains. We reanalyzed the XFMS data to compare polar versus non-polar CheY residue positions. The polar residues around and including the 57D phosphorylated site had an elevated hydroxy radical reactivity. Bioinformatic measures revealed that a water-mediated hydrogen bond network connected this ring of residues with the central 57D. These residues solvated 57D to energetically stabilize the apo-CheY fold. The abundance of these reactive residues was reduced upon activation. This result was supported by the bioinformatics and consistent with the previously reported activation-induced increase in core hydrophobicity. It further illustrated XFMS detection of structural waters. Direct contacts between the ring residues and the phosphorylation site would stabilize the aspartyl phosphate. In addition, we report that the ring residue, 18R, is a constant central node in the 57D solvation network and that 18R non-polar substitutions determine CheY diversity as assessed by its evolutionary trace in bacteria with well-studied chemotaxis. These results showcase the importance of structured water dynamics for phosphorylation-mediated signal transduction.
ISSN:1422-0067
1661-6596
1422-0067
DOI:10.3390/ijms232112771