8XZN
Crystal structure of folE riboswitch with BH4
Summary for 8XZN
| Entry DOI | 10.2210/pdb8xzn/pdb |
| Descriptor | RNA (53-MER), 5,6,7,8-TETRAHYDROBIOPTERIN, MAGNESIUM ION, ... (5 entities in total) |
| Functional Keywords | riboswitch, bh4, rna |
| Biological source | unidentified eubacterium clone A70 |
| Total number of polymer chains | 1 |
| Total formula weight | 17666.24 |
| 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 (1.82 Å) |
Structure validation
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