ArticleJournal of bacteriology2011
S-adenosylmethionine-binding properties of a bacterial phospholipid N-methyltransferase.
Article in Journal of bacteriology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 25 citations in OpenAlex.
- Toward understanding the catalytic mechanism for two classes of bacterial phospholipid N-methyltransferases.The FEBS journal · 2026Article
- The Complexity of erm-Mediated Resistance: Structural and Functional Perspectives From β-Hemolytic Streptococci.Molecular microbiology · 2026Review
- Structural basis for phosphatidylcholine synthesis by bacterial phospholipid N-methyltransferases.The Journal of biological chemistry · 2025Article
- Functional and structural characterization of the human indolethylamine N-methyltransferase through fluorometric, thermal and computational docking analyses.Biology direct · 2025Article
- Development of a multi-epitope vaccine from outer membrane proteins and identification of novel drug targets againstFrontiers in immunology · 2025Article
- Structural insights into phosphatidylethanolamineScience advances · 2024Article
- 16S rRNA Methyltransferases as Novel Drug Targets Against Tuberculosis.The protein journal · 2022Review
- Flagellin lysine methyltransferase FliB catalyzes a [4Fe-4S] mediated methyl transfer reaction.PLoS pathogens · 2021Article
- PhospholipidApplied and environmental microbiology · 2021Article
- Unravelling the Molecular Mechanisms Underlying the Protective Effect of Lactate on the High-Pressure Resistance ofBiomolecules · 2021Article
- SAMbinder: A Web Server for Predicting S-Adenosyl-L-Methionine Binding Residues of a Protein From Its Amino Acid Sequence.Frontiers in pharmacology · 2019Article
- Molecular Basis for Autocatalytic Backbone N-Methylation in RiPP Natural Product Biosynthesis.ACS chemical biology · 2018Article
- Article
- Characterization of a Bvg-regulated fatty acid methyl-transferase in Bordetella pertussis.PloS one · 2017Article
- Membrane lipids in Agrobacterium tumefaciens: biosynthetic pathways and importance for pathogenesis.Frontiers in plant science · 2014Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The presence of the membrane lipid phosphatidylcholine (PC) in the bacterial membrane is critically important for many host-microbe interactions. The phospholipid N-methyltransferase PmtA from the plant pathogen Agrobacterium tumefaciens catalyzes the formation of PC by a three-step methylation of phosphatidylethanolamine via monomethylphosphatidylethanolamine and dimethylphosphatidylethanolamine. The methyl group is provided by S-adenosylmethionine (SAM), which is converted to S-adenosylhomocysteine (SAH) during transmethylation. Despite the biological importance of bacterial phospholipid N-methyltransferases, little is known about amino acids critical for binding to SAM or phospholipids and catalysis. Alanine substitutions in the predicted SAM-binding residues E58, G60, G62, and E84 in A. tumefaciens PmtA dramatically reduced SAM-binding and enzyme activity. Homology modeling of PmtA satisfactorily explained the mutational results. The enzyme is predicted to exhibit a consensus topology of the SAM-binding fold consistent with cofactor interaction as seen with most structurally characterized SAM-methyltransferases. Nuclear magnetic resonance (NMR) titration experiments and (14)C-SAM-binding studies revealed binding constants for SAM and SAH in the low micromolar range. Our study provides first insights into structural features and SAM binding of a bacterial phospholipid N-methyltransferase.
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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.