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methylation confers resistance to more than five classes of clinically used antibiotics, highlighting it as a worrisome mechanism of antibiotic resistance. Here, we report the structure of Cfr, determined by cryogenic electron microscopy (Cryo-EM). Despite its small size (~36 kDa), we exploit a transient protein-RNA crosslink that forms during catalysis, which requires Cys105 to resolve. Using a Cfr Cys105Ala variant and an 87-nucleotide strand of rRNA, we isolate the crosslinked species and determine its structure to 3.0 Å resolution. Notably, the 87-mer rRNA adopts an L-shaped conformation characteristic of tRNAs, rather than the conformation it assumes in the ribosome.
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Olga Esakova
James Jung
Hyunwook Lee
Howard Hughes Medical Institute
University of Pennsylvania
University of Minnesota
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Esakova et al. (Mon,) studied this question.
www.synapsesocial.com/papers/69fef1a2da5c1eb07f2d62df — DOI: https://doi.org/10.64898/2026.02.27.707579