{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Hamid M"],"funding":["National Center for Bigdata and Cloud Computing","Higher Education Commission"],"pagination":["12771"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9659070"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["23(21)"],"pubmed_abstract":["The <i>Escherichia coli</i> 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 b"],"journal":["International journal of molecular sciences"],"pubmed_title":["The Solvation of the <i>E. coli</i> CheY Phosphorylation Site Mapped by XFMS."],"pmcid":["PMC9659070"],"funding_grant_id":["RF-NCBC-015","20-3629/NRPU/R&amp;D/HEC/14/585"],"pubmed_authors":["Khalid MF","Chaudhary SU","Hamid M","Khan S"],"additional_accession":[]},"is_claimable":false,"name":"The Solvation of the <i>E. coli</i> CheY Phosphorylation Site Mapped by XFMS.","description":"The <i>Escherichia coli</i> 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 b","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Oct","modification":"2025-04-04T13:31:26.655Z","creation":"2024-12-04T03:14:51.488Z"},"accession":"S-EPMC9659070","cross_references":{"pubmed":["36361564"],"doi":["10.3390/ijms232112771"]}}