ArticleStructure (London, England : 1993)2008
Multiple-site trimethylation of ribosomal protein L11 by the PrmA methyltransferase.
Article in Structure (London, England : 1993), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- A new target of multiple lysine methylation in bacteria.Journal of bacteriology · 2025Article
- Structural remodeling of AAA+ ATPase p97 by adaptor protein ASPL facilitates posttranslational methylation by METTL21D.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Integrated top-down and bottom-up proteomics mass spectrometry for the characterization of endogenous ribosomal protein heterogeneity.Journal of pharmaceutical analysis · 2023Article
- Substrate recognition by theThe Journal of biological chemistry · 2019Article
- Chemical Biology of Protein N-Terminal Methyltransferases.Chembiochem : a European journal of chemical biology · 2019Review
- The Indispensable Role of Histone MethyltransferaseFrontiers in microbiology · 2019Article
- Interplay of self-association and conformational flexibility in regulating protein function.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Review
- aKMT Catalyzes Extensive Protein Lysine Methylation in the Hyperthermophilic Archaeon Sulfolobus islandicus but is Dispensable for the Growth of the Organism.Molecular & cellular proteomics : MCP · 2016Article
- The METTL20 Homologue from Agrobacterium tumefaciens Is a Dual Specificity Protein-lysine Methyltransferase That Targets Ribosomal Protein L7/L12 and the β Subunit of Electron Transfer Flavoprotein (ETFβ).The Journal of biological chemistry · 2016Article
- The Landscape of Intertwined Associations in Homooligomeric Proteins.Biophysical journal · 2015Review
- Catalytic promiscuity of a bacterial α-N-methyltransferase.FEBS letters · 2012Article
- Substrate and product specificities of SET domain methyltransferases.Epigenetics · 2011Review
- The ribosomal l1 protuberance in yeast is methylated on a lysine residue catalyzed by a seven-beta-strand methyltransferase.The Journal of biological chemistry · 2011Article
- Posttranslational Modifications of Ribosomal Proteins in Escherichia coli.Acta naturae · 2011Article
- Multi-site-specific 16S rRNA methyltransferase RsmF from Thermus thermophilus.RNA (New York, N.Y.) · 2010Article
- Calmodulin methyltransferase is an evolutionarily conserved enzyme that trimethylates Lys-115 in calmodulin.Nature communications · 2010Article
- Structural and functional studies of the Thermus thermophilus 16S rRNA methyltransferase RsmG.RNA (New York, N.Y.) · 2009Article
- Structural rearrangements in the active site of the Thermus thermophilus 16S rRNA methyltransferase KsgA in a binary complex with 5'-methylthioadenosine.Journal of molecular biology · 2009Article
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Authors and funding
4 authors.
Funding
Abstract
Ribosomal protein L11 is a universally conserved component of the large subunit, and plays a significant role during initiation, elongation, and termination of protein synthesis. In Escherichia coli, the lysine methyltransferase PrmA trimethylates the N-terminal alpha-amino group and the epsilon-amino groups of Lys3 and Lys39. Here, we report four PrmA-L11 complex structures in different orientations with respect to the PrmA active site. Two structures capture the L11 N-terminal alpha-amino group in the active site in a trimethylated post-catalytic state and in a dimethylated state with bound S-adenosyl-L-homocysteine. Two other structures show L11 in a catalytic orientation to modify Lys39 and in a noncatalytic orientation. The comparison of complex structures in different orientations with a minimal substrate recognition complex shows that the binding mode remains conserved in all L11 orientations, and that substrate orientation is brought about by the unusual interdomain flexibility of PrmA.
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