Structural highlights
FunctionRL7A_PYRFU Multifunctional RNA-binding protein that recognizes the K-turn motif in ribosomal RNA, box H/ACA, box C/D and box C'/D' sRNAs (By similarity). Publication Abstract from PubMedSolid-state NMR (ssNMR) is applicable to high molecular-weight (MW) protein assemblies in a non-amorphous precipitate. The technique yields atomic resolution structural information on both soluble and insoluble particles without limitations of MW or requirement of sizeable crystals. Recently, we expanded the application of ssNMR to nucleic acids and solved the first de novo structure of RNA by ssNMR. Here, we propose and demonstrate an approach that yields the structure of protein-RNA complexes (RNP) from solely ssNMR data. Instead of using low-sensitivity magnetization transfer steps between heteronuclei of the protein and the RNA, we measure paramagnetic relaxation enhancement effects elicited on the RNA by a paramagnetic tag coupled to the protein. We demonstrate that this data, together with chemical-shift-perturbation data, yields an accurate structure of an RNP complex, starting from the bound structures of its components, which have been determined by established methodology. The possibility of characterizing RNA-protein interactions by ssNMR enables a plethora of applications to large RNP complexes, whose structure is not accessible from other methods. Structure of a protein-RNA complex by ssNMR.,Carlomagno T, Ahmed M, Marchanka A Angew Chem Int Ed Engl. 2020 Feb 5. doi: 10.1002/anie.201915465. PMID:32023357[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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