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Title: Structural Basis for Methyl Transfer by a Radical SAM Enzyme

Abstract

The radical S-adenosyl-l-methionine (SAM) enzymes RlmN and Cfr methylate 23S ribosomal RNA, modifying the C2 or C8 position of adenosine 2503. The methyl groups are installed by a two-step sequence involving initial methylation of a conserved Cys residue (RlmN Cys{sup 355}) by SAM. Methyl transfer to the substrate requires reductive cleavage of a second equivalent of SAM. Crystal structures of RlmN and RlmN with SAM show that a single molecule of SAM coordinates the [4Fe-4S] cluster. Residue Cys{sup 355} is S-methylated and located proximal to the SAM methyl group, suggesting the SAM that is involved in the initial methyl transfer binds at the same site. Thus, RlmN accomplishes its complex reaction with structural economy, harnessing the two most important reactivities of SAM within a single site.

Authors:
; ; ; ; ;  [1]
  1. NWU
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
National Institutes of Health (NIH)
OSTI Identifier:
1020581
Resource Type:
Journal Article
Journal Name:
Science
Additional Journal Information:
Journal Volume: 332; Journal Issue: 05, 2011; Journal ID: ISSN 0193-4511
Country of Publication:
United States
Language:
ENGLISH
Subject:
59 BASIC BIOLOGICAL SCIENCES; 99 GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE; ADENOSINE; CLEAVAGE; CRYSTAL STRUCTURE; ENZYMES; METHYLATION; RADICALS; RESIDUES; RIBOSOMAL RNA; SUBSTRATES

Citation Formats

Boal, Amie K., Grove, Tyler L., McLaughlin, Monica I., Yennawar, Neela H., Booker, Squire J., Rosenzweig, Amy C., and Penn). Structural Basis for Methyl Transfer by a Radical SAM Enzyme. United States: N. p., 2014. Web. doi:10.1126/science.1205358.
Boal, Amie K., Grove, Tyler L., McLaughlin, Monica I., Yennawar, Neela H., Booker, Squire J., Rosenzweig, Amy C., & Penn). Structural Basis for Methyl Transfer by a Radical SAM Enzyme. United States. https://doi.org/10.1126/science.1205358
Boal, Amie K., Grove, Tyler L., McLaughlin, Monica I., Yennawar, Neela H., Booker, Squire J., Rosenzweig, Amy C., and Penn). 2014. "Structural Basis for Methyl Transfer by a Radical SAM Enzyme". United States. https://doi.org/10.1126/science.1205358.
@article{osti_1020581,
title = {Structural Basis for Methyl Transfer by a Radical SAM Enzyme},
author = {Boal, Amie K. and Grove, Tyler L. and McLaughlin, Monica I. and Yennawar, Neela H. and Booker, Squire J. and Rosenzweig, Amy C. and Penn)},
abstractNote = {The radical S-adenosyl-l-methionine (SAM) enzymes RlmN and Cfr methylate 23S ribosomal RNA, modifying the C2 or C8 position of adenosine 2503. The methyl groups are installed by a two-step sequence involving initial methylation of a conserved Cys residue (RlmN Cys{sup 355}) by SAM. Methyl transfer to the substrate requires reductive cleavage of a second equivalent of SAM. Crystal structures of RlmN and RlmN with SAM show that a single molecule of SAM coordinates the [4Fe-4S] cluster. Residue Cys{sup 355} is S-methylated and located proximal to the SAM methyl group, suggesting the SAM that is involved in the initial methyl transfer binds at the same site. Thus, RlmN accomplishes its complex reaction with structural economy, harnessing the two most important reactivities of SAM within a single site.},
doi = {10.1126/science.1205358},
url = {https://www.osti.gov/biblio/1020581}, journal = {Science},
issn = {0193-4511},
number = 05, 2011,
volume = 332,
place = {United States},
year = {Thu Oct 02 00:00:00 EDT 2014},
month = {Thu Oct 02 00:00:00 EDT 2014}
}