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• W2000627319 endingPage "493" @default.
• W2000627319 startingPage "487" @default.
• W2000627319 abstract "The E. coli Rho protein disengages newly transcribed RNA from its DNA template, helping terminate certain transcripts. We have determined the X-ray crystal structure of the RNA-binding domain of Rho complexed to an RNA ligand. Filters that screen both ligand size and chemical functionality line the primary nucleic acid–binding site, imparting sequence specificity to a generic single-stranded nucleic acid–binding fold and explaining the preference of Rho for cytosine-rich RNA. The crystal packing reveals two Rho domain protomers bound to a single RNA with a single base spacer, suggesting that the strong RNA-binding sites of Rho may arise from pairing of RNA-binding modules. Dimerization of symmetric subunits on an asymmetric ligand is developed as a model for allosteric control in the action of the intact Rho hexamer." @default.
• W2000627319 created "2016-06-24" @default.
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• W2000627319 date "1999-04-01" @default.
• W2000627319 modified "2023-10-15" @default.
• W2000627319 title "The Structural Basis for Terminator Recognition by the Rho Transcription Termination Factor" @default.
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• W2000627319 doi "https://doi.org/10.1016/s1097-2765(00)80476-1" @default.
• W2000627319 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/10230401" @default.
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