5HR7

X-ray crystal structure of C118A RlmN from Escherichia coli with cross-linked in vitro transcribed tRNA

Summary for 5HR7

• Entry DOI: 10.2210/pdb5hr7/pdb
• Related: 5HR6
• Descriptor: tRNA Glu, Dual-specificity RNA methyltransferase RlmN, MAGNESIUM ION, ... (7 entities in total)
• Functional Keywords: protein-rna complex, radical sam enzyme, transfer rna, iron-sulfur cluster, oxidoreductase-rna complex, oxidoreductase/rna
• Biological source: Escherichia coli; More
• Cellular location: Cytoplasm : A7ZPW0
• Total number of polymer chains: 4
• Total formula weight: 141232.88

Authors

Schwalm, E.L.,Grove, T.L.,Booker, S.J.,Boal, A.K. (deposition date: 2016-01-22, release date: 2016-04-13, Last modification date: 2024-10-16)

Primary citation

Schwalm, E.L.,Grove, T.L.,Booker, S.J.,Boal, A.K.
Crystallographic capture of a radical S-adenosylmethionine enzyme in the act of modifying tRNA.
Science, 352:309-312, 2016

PubMed 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(118)→Ala variant of the protein is cross-linked to a tRNA(Glu)substrate through the terminal methylene carbon of a formerly methylcysteinyl residue and C2 of A37. RlmN contacts the entire length of tRNA(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.

PubMed: 27081063
DOI: 10.1126/science.aad5367

Experimental method

X-RAY DIFFRACTION (2.4 Å)