Crystallographic capture of a radical S -adenosylmethionine enzyme in the act of modifying tRNA

Author:

Schwalm Erica L.1,Grove Tyler L.1,Booker Squire J.123,Boal Amie K.12

Affiliation:

1. Department of Chemistry, Pennsylvania State University, University Park, PA 16802, USA.

2. Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, PA 16802, USA.

3. Howard Hughes Medical Institute, Pennsylvania State University, University Park, PA 16802, USA.

Abstract

An RNA methylase caught in the act RNA methylation is important in RNA function and in antibiotic resistance. The RNA methylase RlmN is a dual-specificity enzyme that can act on ribosomal and transfer RNA (tRNA). RlmN is a radical S-adenosylmethionine (SAM) enzyme, which produces a protein/RNA cross-linked intermediate. Schwalm et al. determined the structure of RlmN cross-linked to a tRNA substrate and found that the enzyme recognizes the overall shape of the tRNA. Then it remodels the anticodon region to access the base that it methylates. The remodeling activity is likely to be key to the enzyme's dual specificity. Science , this issue p. 309

Funder

NIH

Searle Scholars Program

Tobacco Settlement Funds

U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences

Michigan Economic Development Corporation

Michigan Technology Tri-Corridor

National Cancer Institute

National Institute of General Medical Science

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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