ArticleScience (New York, N.Y.)2011
Structural basis for methyl transfer by a radical SAM enzyme.
Article in Science (New York, N.Y.), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
90 citing papers in PubMed.
- Beyond native reactivity: radical SAM enzymes as platforms for new-to-nature chemistry.RSC chemical biology · 2026Review
- Structural and Spectroscopic Basis for Catalysis by a Class C RadicalJournal of the American Chemical Society · 2026Article
- Structural Basis for CbioRxiv : the preprint server for biology · 2026Article
- Structural and Spectroscopic Basis for Catalysis by a Class C RadicalbioRxiv : the preprint server for biology · 2026Article
- A Frameshift Mutation in the MethyltransferaseComputational and structural biotechnology journal · 2026Article
- Ribosomal RNA modification enzymes stimulate large ribosome subunit assembly in E. coli.Nucleic acids research · 2024Article
- Structural and mechanistic basis for RiPP epimerization by a radical SAM enzyme.Nature chemical biology · 2024Article
- CNature communications · 2024Article
- Cluster-selectiveChemical science · 2023Article
- Ribosome-targeting antibiotics and resistanceRSC medicinal chemistry · 2023Review
- Facile and dynamic cleavage of every iron-sulfide bond in cuboidal iron-sulfur clusters.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Structure and Catalytic Mechanism of Radical SAM Methylases.Life (Basel, Switzerland) · 2022Review
- Radical SAM-dependent formation of a nitrogenase cofactor core on NifB.Journal of inorganic biochemistry · 2022Review
- Functional Diversity of HemN-like Proteins.ACS bio & med chem Au · 2022Review
- Directed evolution of the rRNA methylating enzyme Cfr reveals molecular basis of antibiotic resistance.eLife · 2022Article
- Eukaryotic TYW1 Is a Radical SAM Flavoenzyme.Biochemistry · 2021Article
- X-Ray Crystallographic Analysis of NifB with a Full Complement of Clusters: Structural Insights into the Radical SAM-Dependent Carbide Insertion During Nitrogenase Cofactor Assembly.Angewandte Chemie (International ed. in English) · 2021Article
- miCLIP-MaPseq Identifies Substrates of Radical SAM RNA-Methylating Enzyme Using Mechanistic Cross-Linking and Mismatch Profiling.Methods in molecular biology (Clifton, N.J.) · 2021Article
- New Perspectives of S-Adenosylmethionine (SAMe) Applications to Attenuate Fatty Acid-Induced Steatosis and Oxidative Stress in Hepatic and Endothelial Cells.Molecules (Basel, Switzerland) · 2020Article
- Biosynthesis of Nitrogenase Cofactors.Chemical reviews · 2020Review
30 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
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(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(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.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.