Publication Date:
2016-04-16
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schwalm, Erica L -- Grove, Tyler L -- Booker, Squire J -- Boal, Amie K -- GM100011/GM/NIGMS NIH HHS/ -- GM101957/GM/NIGMS NIH HHS/ -- Y1-CO-1020/CO/NCI NIH HHS/ -- Y1-GM-1104/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2016 Apr 15;352(6283):309-12. doi: 10.1126/science.aad5367.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Pennsylvania State University, University Park, PA 16802, USA. ; Department of Chemistry, Pennsylvania State University, University Park, PA 16802, USA. Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, PA 16802, USA. Howard Hughes Medical Institute, Pennsylvania State University, University Park, PA 16802, USA. squire@psu.edu akb20@psu.edu. ; Department of Chemistry, Pennsylvania State University, University Park, PA 16802, USA. Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, PA 16802, USA. squire@psu.edu akb20@psu.edu.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/27081063" target="_blank"〉PubMed〈/a〉
Keywords:
Adenosine/chemistry
;
Alanine/chemistry/genetics
;
Amino Acid Substitution
;
Anticodon/chemistry
;
Catalytic Domain
;
Crystallography, X-Ray
;
Cysteine/chemistry/genetics
;
Escherichia coli Proteins/*chemistry/genetics/*ultrastructure
;
Methylation
;
Methyltransferases/*chemistry/genetics/*ultrastructure
;
Nucleic Acid Conformation
;
Protein Structure, Tertiary
;
RNA, Bacterial/*chemistry
;
RNA, Transfer, Glu/*chemistry/*ultrastructure
;
S-Adenosylmethionine/chemistry
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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