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8XZL

Crystal structure of folE riboswitch with DHF

Summary for 8XZL
Entry DOI10.2210/pdb8xzl/pdb
DescriptorRNA (53-MER), DIHYDROFOLIC ACID, MAGNESIUM ION, ... (5 entities in total)
Functional Keywordsriboswitch, dhf, rna
Biological sourceunidentified eubacterium clone A70
Total number of polymer chains1
Total formula weight17917.02
Authors
Li, C.Y.,Ren, A.M. (deposition date: 2024-01-21, release date: 2024-07-24, Last modification date: 2024-08-21)
Primary citationLi, 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: 38769061
DOI: 10.1093/nar/gkae377
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.13 Å)
Structure validation

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