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• W2062808839 startingPage "372" @default.
• W2062808839 abstract "The trp RNA-binding attenuation protein (TRAP) is a paradigmatic allosteric protein that regulates the tryptophan biosynthetic genes associated with the trp operon in bacilli. The ring-shaped 11-mer TRAP is activated for recognition of a specific trp-mRNA target by binding up to 11 tryptophan molecules. To characterize the mechanisms of tryptophan-induced TRAP activation, we have performed methyl relaxation dispersion (MRD) nuclear magnetic resonance (NMR) experiments that probe the time-dependent structure of TRAP in the microsecond-to-millisecond chemical exchange time window. We find significant side chain flexibility localized to the RNA and tryptophan binding sites of the apo protein and that these dynamics are dramatically reduced upon ligand binding. Analysis of the MRD NMR data provides insights into the structural nature of transiently populated conformations sampled in solution by apo TRAP. The MRD data are inconsistent with global two-state exchange, indicating that conformational sampling in apo TRAP is asynchronous. These findings imply a temporally heterogeneous population of structures that are incompatible with RNA binding and substantiate the study of TRAP as a paradigm for probing and understanding essential dynamics in allosteric, regulatory proteins." @default.
• W2062808839 created "2016-06-24" @default.
• W2062808839 creator A5013174279 @default.
• W2062808839 creator A5079546510 @default.
• W2062808839 creator A5082288662 @default.
• W2062808839 date "2012-01-01" @default.
• W2062808839 modified "2023-09-29" @default.
• W2062808839 title "Mechanisms of Allosteric Gene Regulation by NMR Quantification of Microsecond–Millisecond Protein Dynamics" @default.
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• W2062808839 doi "https://doi.org/10.1016/j.jmb.2011.11.019" @default.
• W2062808839 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3258336" @default.
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