8XZQ
Crystal structure of folE riboswitch with 8-N Guanine
Summary for 8XZQ
Entry DOI | 10.2210/pdb8xzq/pdb |
Descriptor | RNA (53-MER), 5-AMINO-1H-[1,2,3]TRIAZOLO[4,5-D]PYRIMIDIN-7-OL, SPERMINE, ... (5 entities in total) |
Functional Keywords | riboswitch, 8-n guanine, rna |
Biological source | unidentified eubacterium clone A70 |
Total number of polymer chains | 1 |
Total formula weight | 17698.63 |
Authors | |
Primary citation | Li, C.,Xu, X.,Geng, Z.,Zheng, L.,Song, Q.,Shen, X.,Wu, J.,Zhao, J.,Li, H.,He, M.,Tai, X.,Zhang, L.,Ma, J.,Dong, Y.,Ren, A. Structure-based characterization and compound identification of the wild-type THF class-II riboswitch. Nucleic Acids Res., 52:8454-8465, 2024 Cited by PubMed Abstract: Riboswitches are conserved regulatory RNA elements participating in various metabolic pathways. Recently, a novel RNA motif known as the folE RNA motif was discovered upstream of folE genes. It specifically senses tetrahydrofolate (THF) and is therefore termed THF-II riboswitch. To unravel the ligand recognition mechanism of this newly discovered riboswitch and decipher the underlying principles governing its tertiary folding, we determined both the free-form and bound-form THF-II riboswitch in the wild-type sequences. Combining structural information and isothermal titration calorimetry (ITC) binding assays on structure-based mutants, we successfully elucidated the significant long-range interactions governing the function of THF-II riboswitch and identified additional compounds, including alternative natural metabolites and potential lead compounds for drug discovery, that interact with THF-II riboswitch. Our structural research on the ligand recognition mechanism of the THF-II riboswitch not only paves the way for identification of compounds targeting riboswitches, but also facilitates the exploration of THF analogs in diverse biological contexts or for therapeutic applications. PubMed: 38769061DOI: 10.1093/nar/gkae377 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.83 Å) |
Structure validation
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