Crystallographic capture of a radical S-adenosylmethionine enzyme in the act of modifying tRNA.
Crystallographic capture of a radical S-adenosylmethionine enzyme in the act of modifying tRNA.
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DOI：
10.1126/science.aad5367
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发表时间：
2016-04-15
期刊：
影响因子：
--
通讯作者：
Boal AK
中科院分区：
文献类型：
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作者：
Schwalm EL;Grove TL;Booker SJ;Boal AK
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 tRNAs. A related methylase, Cfr, modifies C8 of A2503 by a similar mechanism, conferring resistance to multiple classes of antibiotics. Herein, 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 using an induced-fit strategy that completely unfolds the tRNA anticodon stem loop, which is likely critical for recognition of both tRNA and rRNA substrates.
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DOI：
10.1126/science.1205358
发表时间：
2011-05-27
期刊：
Science (New York, N.Y.)
影响因子：
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作者：
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DOI：
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发表时间：
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期刊：
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影响因子：
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作者：
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