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• W2154379876 abstract "The second messenger signaling molecule bis-(3'-5')-cyclic dimeric guanosine monophosphate (c-di-GMP) regulates many processes in bacteria, including motility, pathogenesis and biofilm formation. c-di-GMP-binding riboswitches are important downstream targets in this signaling pathway. Here we report the crystal structure, at 2.7 A resolution, of a c-di-GMP riboswitch aptamer from Vibrio cholerae bound to c-di-GMP, showing that the ligand binds within a three-helix junction that involves base-pairing and extensive base-stacking. The symmetric c-di-GMP is recognized asymmetrically with respect to both the bases and the backbone. A mutant aptamer was engineered that preferentially binds the candidate signaling molecule c-di-AMP over c-di-GMP. Kinetic and structural data suggest that genetic regulation by the c-di-GMP riboswitch is kinetically controlled and that gene expression is modulated through the stabilization of a previously unidentified P1 helix, illustrating a direct mechanism for c-di-GMP signaling." @default.
• W2154379876 created "2016-06-24" @default.
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• W2154379876 date "2009-11-08" @default.
• W2154379876 modified "2023-09-23" @default.
• W2154379876 title "Structural basis of ligand binding by a c-di-GMP riboswitch" @default.
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• W2154379876 doi "https://doi.org/10.1038/nsmb.1702" @default.
• W2154379876 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2850612" @default.
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