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• W2060289339 abstract "DNA-binding response regulators (RRs) of the OmpR/PhoB subfamily alternate between inactive and active conformational states, with the latter having enhanced DNA-binding affinity. Phosphorylation of an aspartate residue in the receiver domain, usually via phosphotransfer from a cognate histidine kinase, stabilizes the active conformation. Many of the available structures of inactive OmpR/PhoB family proteins exhibit extensive interfaces between the N-terminal receiver and C-terminal DNA-binding domains. These interfaces invariably involve the α4-β5-α5 face of the receiver domain, the locus of the largest differences between inactive and active conformations and the surface that mediates dimerization of receiver domains in the active state. Structures of receiver domain dimers of DrrB, DrrD, and MtrA have been determined, and phosphorylation kinetics were analyzed. Analysis of phosphotransfer from small molecule phosphodonors has revealed large differences in autophosphorylation rates among OmpR/PhoB RRs. RRs with substantial domain interfaces exhibit slow rates of phosphorylation. Rates are greatly increased in isolated receiver domain constructs. Such differences are not observed between autophosphorylation rates of full-length and isolated receiver domains of a RR that lacks interdomain interfaces, and they are not observed in histidine kinase-mediated phosphotransfer. These findings suggest that domain interfaces restrict receiver domain conformational dynamics, stabilizing an inactive conformation that is catalytically incompetent for phosphotransfer from small molecule phosphodonors. Inhibition of phosphotransfer by domain interfaces provides an explanation for the observation that some RRs cannot be phosphorylated by small molecule phosphodonors in vitro and provides a potential mechanism for insulating some RRs from small molecule-mediated phosphorylation in vivo. DNA-binding response regulators (RRs) of the OmpR/PhoB subfamily alternate between inactive and active conformational states, with the latter having enhanced DNA-binding affinity. Phosphorylation of an aspartate residue in the receiver domain, usually via phosphotransfer from a cognate histidine kinase, stabilizes the active conformation. Many of the available structures of inactive OmpR/PhoB family proteins exhibit extensive interfaces between the N-terminal receiver and C-terminal DNA-binding domains. These interfaces invariably involve the α4-β5-α5 face of the receiver domain, the locus of the largest differences between inactive and active conformations and the surface that mediates dimerization of receiver domains in the active state. Structures of receiver domain dimers of DrrB, DrrD, and MtrA have been determined, and phosphorylation kinetics were analyzed. Analysis of phosphotransfer from small molecule phosphodonors has revealed large differences in autophosphorylation rates among OmpR/PhoB RRs. RRs with substantial domain interfaces exhibit slow rates of phosphorylation. Rates are greatly increased in isolated receiver domain constructs. Such differences are not observed between autophosphorylation rates of full-length and isolated receiver domains of a RR that lacks interdomain interfaces, and they are not observed in histidine kinase-mediated phosphotransfer. These findings suggest that domain interfaces restrict receiver domain conformational dynamics, stabilizing an inactive conformation that is catalytically incompetent for phosphotransfer from small molecule phosphodonors. Inhibition of phosphotransfer by domain interfaces provides an explanation for the observation that some RRs cannot be phosphorylated by small molecule phosphodonors in vitro and provides a potential mechanism for insulating some RRs from small molecule-mediated phosphorylation in vivo." @default.
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• W2060289339 date "2010-10-01" @default.
• W2060289339 modified "2023-10-12" @default.
• W2060289339 title "Regulation of Response Regulator Autophosphorylation through Interdomain Contacts" @default.
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• W2060289339 cites W1934365823 @default.
• W2060289339 cites W1963619815 @default.
• W2060289339 cites W1967494222 @default.
• W2060289339 cites W1975008340 @default.
• W2060289339 cites W1978024591 @default.
• W2060289339 cites W1983358200 @default.
• W2060289339 cites W1985260825 @default.
• W2060289339 cites W1985382340 @default.
• W2060289339 cites W1986191025 @default.
• W2060289339 cites W1994076348 @default.
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• W2060289339 cites W2000114467 @default.
• W2060289339 cites W2001641653 @default.
• W2060289339 cites W2002099745 @default.
• W2060289339 cites W2007844210 @default.
• W2060289339 cites W2011970304 @default.
• W2060289339 cites W2026677195 @default.
• W2060289339 cites W2028968631 @default.
• W2060289339 cites W2035135843 @default.
• W2060289339 cites W2044046412 @default.
• W2060289339 cites W2045143386 @default.
• W2060289339 cites W2046002103 @default.
• W2060289339 cites W2048822589 @default.
• W2060289339 cites W2049245598 @default.
• W2060289339 cites W2053004995 @default.
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• W2060289339 cites W2066962978 @default.
• W2060289339 cites W2069348244 @default.
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• W2060289339 cites W2083726121 @default.
• W2060289339 cites W2084001324 @default.
• W2060289339 cites W2088880573 @default.
• W2060289339 cites W2090654767 @default.
• W2060289339 cites W2093980244 @default.
• W2060289339 cites W2106531843 @default.
• W2060289339 cites W2108559568 @default.
• W2060289339 cites W2110343075 @default.
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• W2060289339 doi "https://doi.org/10.1074/jbc.m110.157164" @default.
• W2060289339 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2952233" @default.
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