Structural highlights
Publication Abstract from PubMedThe widespread ykkC-I riboswitch class exemplifies divergent riboswitch evolution. To analyze how natural selection has diversified its versatile RNA fold, we determined the X-ray crystal structure of the Burkholderia sp. TJI49 ykkC-I subtype-1 (Guanidine-I) riboswitch aptamer domain. Differing from the previously reported structures of orthologs from Dickeya dadantii and Sulfobacillus acidophilus, our Burkholderia structure reveals a chelated K(+) ion adjacent to two Mg(2+) ions in the guanidine-binding pocket. Thermal melting analysis shows that K(+) chelation, which induces localized conformational changes in the binding pocket, improves guanidinium-RNA interactions. Analysis of ribosome structures suggests that the [K(+)(Mg(2+))2] ion triad is uncommon. It is, however, reminiscent of metal ion clusters found in the active sites of ribozymes and DNA polymerases. Previous structural characterization of ykkC-I subtype-2 RNAs, which bind the effector ligands ppGpp and PRPP, indicate that in those paralogs, an adenine responsible for K(+) chelation in the Burkholderia Guanidine-I riboswitch is replaced by a pyrimidine. This mutation results in a water molecule and Mg(2+) ion binding in place of the K(+) ion. Thus, our structural analysis demonstrates how ion and solvent chelation tune divergent ligand specificity and affinity among ykkC-I riboswitches. An uncommon [K(+)(Mg(2+))2] metal ion triad imparts stability and selectivity to the Guanidine-I riboswitch.,Trachman RJ 3rd, Ferre-D'Amare AR RNA. 2021 Oct;27(10):1257-1264. doi: 10.1261/rna.078824.121. Epub 2021 Jul 13. PMID:34257148[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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