9l6z
From Proteopedia
Crystal structure of the L7Ae derivative protein LS12 in RNA-free state
Structural highlights
FunctionRL7A_ARCFU Multifunctional RNA-binding protein that recognizes the K-turn motif in ribosomal RNA, box H/ACA and box C/D sRNAs.[1] Publication Abstract from PubMedCS1-LS4 and CS2-LS12 are ultra-high affinity and orthogonal RNA-protein pairs that were identified by PD-SELEX (Phage Display coupled with Systematic Evolution of Ligands by EXponential enrichment). To investigate the molecular basis of the lab-coevolved RNA-RBP pairs, we determined the structures of the CS1-LS4 and CS2-LS12 complexes and the LS12 homodimer in an RNA-free state by X-ray crystallography. The structural analyses revealed that the lab-coevolved RNA-RBPs have acquired unique molecular recognition mechanisms, whereas the overall structures of the RNP complexes were similar to the typical kink-turn RNA-L7Ae complex. The orthogonal RNA-RBP pairs were applied to construct high-performance cell-free riboswitches that regulate translation in response to LS4 or LS12. In addition, by using the orthogonal protein-responsive switches, we generated an AND logic gate that outputs staphylococcal gamma-hemolysin in cell-free system and carried out hemolysis assay and calcein leakage assay using rabbit red blood cells and artificial cells, respectively. Structural insights into lab-coevolved RNA-RBP pairs and applications of synthetic riboswitches in cell-free system.,Fukunaga K, Teramoto T, Nakashima M, Ohtani T, Katsuki R, Matsuura T, Yokobayashi Y, Kakuta Y Nucleic Acids Res. 2025 Mar 20;53(6):gkaf212. doi: 10.1093/nar/gkaf212. PMID:40119732[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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