ArticleBiochemistry2016
Burkholderia glumae ToxA Is a Dual-Specificity Methyltransferase That Catalyzes the Last Two Steps of Toxoflavin Biosynthesis.
Article in Biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 23 citations in OpenAlex.
- Structural Revision of the CAngewandte Chemie (International ed. in English) · 2026Article
- High-Throughput Prediction of Protein-Protein Interactions Uncovers Hidden Molecular Networks in Biosynthetic Gene Clusters.Computational and structural biotechnology journal · 2026Article
- Inhibitory effects of reumycin produced by Streptomyces sp. TPMA0082 on virulence factors of Pseudomonas aeruginosa.Journal of natural medicines · 2025Article
- Exquisite Complex Reaction Cascade in the Natural 1,2,4-Triazine Assembly.Journal of the American Chemical Society · 2025Article
- Crystal Structure, Modeling, and Identification of Key Residues Provide Insights into the Mechanism of the Key Toxoflavin Biosynthesis Protein ToxD.Biochemistry · 2025Article
- Unlocking the potential of bacterial endophytes from medicinal plants for drug discovery.Microbial biotechnology · 2024Review
- UnderstandingPlants (Basel, Switzerland) · 2023Article
- tepR encoding a bacterial enhancer-binding protein orchestrates the virulence and interspecies competition of Burkholderia glumae through qsmR and a type VI secretion system.Molecular plant pathology · 2020Article
- Bioactivity-HiTES Unveils Cryptic Antibiotics Encoded in Actinomycete Bacteria.ACS chemical biology · 2019Article
- Article
- Heteroatom-Heteroatom Bond Formation in Natural Product Biosynthesis.Chemical reviews · 2017Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Toxoflavin is a major virulence factor of the rice pathogen Burkholderia glumae. The tox operon of B. glumae contains five putative toxoflavin biosynthetic genes toxABCDE. ToxA is a predicted S-adenosylmethionine-dependent methyltransferase, and toxA knockouts of B. glumae are less virulent in plant infection models. In this study, we show that ToxA performs two consecutive methylations to convert the putative azapteridine intermediate, 1,6-didemethyltoxoflavin, to toxoflavin. In addition, we report a series of crystal structures of ToxA complexes that reveals the molecular basis of the dual methyltransferase activity. The results suggest sequential methylations with initial methylation at N6 of 1,6-didemethyltoxoflavin followed by methylation at N1. The two azapteridine orientations that position N6 or N1 for methylation are coplanar with a 140° rotation between them. The structure of ToxA contains a class I methyltransferase fold having an N-terminal extension that either closes over the active site or is largely disordered. The ordered conformation places Tyr7 at a position of a structurally conserved tyrosine site of unknown function in various methyltransferases. Crystal structures of ToxA-Y7F consistently show a closed active site, whereas structures of ToxA-Y7A consistently show an open active site, suggesting that the hydroxyl group of Tyr7 plays a role in opening and closing the active site during the multistep reaction.
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