Crystallographic capture of a radical S-adenosylmethionine enzyme in the act of modifying tRNA
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Author(s)
Schwalm, E. L.
Grove, T. L.
Boal, A. K.
Booker, Squire J.
Date Issued
April 2016
Journal
Science
Publisher
American Association for the Advancement of Science (AAAS)
Citation
Schwalm, E. L., et al. “Crystallographic Capture of a Radical S-Adenosylmethionine Enzyme in the Act of Modifying TRNA.” Science, vol. 352, no. 6283, Apr. 2016, pp. 309–12.
Version
Author's final manuscript
Abstract
RlmN is a dual-specificity RNA methylase that modifies C2 of adenosine 2503 (A2503) in 23S rRNA and C2 of adenosine 37 (A37) in several Escherichia coli transfer RNAs (tRNAs). A related methylase, Cfr, modifies C8 of A2503 via a similar mechanism, conferring resistance to multiple classes of antibiotics. Here, we report the x-ray structure of a key intermediate in the RlmN reaction, in which a Cys[superscript 118]→Ala variant of the protein is cross-linked to a tRNA[superscript Glu] substrate through the terminal methylene carbon of a formerly methylcysteinyl residue and C2 of A37. RlmN contacts the entire length of tRNA[superscript Glu], accessing A37 by using an induced-fit strategy that completely unfolds the tRNA anticodon stem-loop, which is likely critical for recognition of both tRNA and ribosomal RNA substrates.
MIT Department
Massachusetts Institute of Technology. Department of Chemistry
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DOI of Published Version
https://doi.org/10.1126/SCIENCE.AAD5367
