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Publication Abstract from PubMed

The widespread oligonucleotide/oligosaccharide-binding (OB)-fold recognizes diverse substrates from sugars to nucleic acids and proteins, and plays key roles in genome maintenance, transcription, translation, and tRNA metabolism. OB-containing bacterial Trbp and yeast Arc1p proteins are thought to recognize the tRNA elbow or anticodon regions. Here we report a 2.6 A co-crystal structure of Aquifex aeolicus Trbp111 bound to tRNA(Ile), which reveals that Trbp recognizes tRNAs solely by capturing their 3' ends. Structural, mutational, and biophysical analyses show that the Trbp/EMAPII-like OB fold precisely recognizes the single-stranded structure, 3' terminal location, and specific sequence of the 3' CA dinucleotide - a universal feature of mature tRNAs. Arc1p supplements its OB - tRNA 3' end interaction with additional contacts that involve an adjacent basic region and the tRNA body. This study uncovers a previously unrecognized mode of tRNA recognition by an ancient protein fold, and provides insights into protein-mediated tRNA aminoacylation, folding, localization, trafficking, and piracy.

Structural basis of tRNA recognition by the widespread OB fold.,Umuhire Juru A, Ghirlando R, Zhang J Nat Commun. 2024 Jul 29;15(1):6385. doi: 10.1038/s41467-024-50730-1. PMID:39075051^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.