@article{05fc8f9fd40b4d92a02b29964952d6cc,
title = "Crystallographic capture of a radical S-adenosylmethionine enzyme in the act of modifying tRNA",
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 Cys118→Ala variant of the protein is cross-linked to a tRNAGlu substrate through the terminal methylene carbon of a formerly methylcysteinyl residue and C2 of A37. RlmN contacts the entire length of tRNAGlu, 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.",
author = "Schwalm, {Erica L.} and Grove, {Tyler L.} and Booker, {Squire J.} and Boal, {Amie K.}",
note = "Funding Information: This work has been supported by NIH grants GM100011 (A.K.B.) and GM101957 (S.J.B.), the Searle Scholars Program (A.K.B.), and Tobacco Settlement Funds (TSF13/14 SAP-4100062216) to S.J.B. Use of the Advanced Photon Source was supported by the U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences, under contract DE-AC02-06CH11357. Use of the LS-CAT Sector 21 was supported by the Michigan Economic Development Corporation and the Michigan Technology Tri-Corridor (grant 085P1000817). GM/CA-CAT has been funded in whole or in part with federal funds from the National Cancer Institute (Y1-CO-1020) and the National Institute of General Medical Science (Y1-GM-1104). Coordinates and structure factors have been deposited in the Protein Data Bank (PDB) with accession codes 5HR6 (C118A RlmN/tRNA in vivo cross-link) and 5HR7(C118A RlmN/tRNA in vitro cross-link). Publisher Copyright: {\textcopyright} 2016, American Association for the Advancement of Science. All rights reserved.",
year = "2016",
month = apr,
day = "15",
doi = "10.1126/science.aad5367",
language = "English (US)",
volume = "352",
pages = "309--312",
journal = "Science",
issn = "0036-8075",
publisher = "American Association for the Advancement of Science",
number = "6283",
}