ArticleCell research2022
Crystal structure and catalytic mechanism of the MbnBC holoenzyme required for methanobactin biosynthesis.
Article in Cell research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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33 citing papers in PubMed, 44 citations in OpenAlex.
- Bis-hydroxylation of Homocitrulline Catalyzed by a Multinuclear Nonheme Iron Oxidative Enzyme during RiPP Biosynthesis.Journal of the American Chemical Society · 2026Article
- Thiooxazole Formation on a NontypeablebioRxiv : the preprint server for biology · 2026Article
- Unveiling Putative Functions of Burkholderia pseudomallei K96243 Hypothetical Proteins Via High-Throughput Characterization of Structural Similarities.Interdisciplinary sciences, computational life sciences · 2026Article
- Bis-hydroxylation of Homocitrulline Catalyzed by a Multinuclear Nonheme Iron-Dependent Oxidative Enzyme during RiPP Biosynthesis.bioRxiv : the preprint server for biology · 2026Article
- Biosynthesis of Peptidic Thiooxazole Metallophores Installed by Multinuclear Nonheme Iron Enzymes.ACS chemical biology · 2026Article
- Co-opting the bacterial lipoprotein pathway for the biosynthesis of lipidated macrocyclic peptides.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Oxidative Peptide Backbone Cleavage by a HEXXH Enzyme during RiPP Biosynthesis.Journal of the American Chemical Society · 2026Article
- Oxidative Peptide Backbone Cleavage by a HEXXH Enzyme During RiPP Biosynthesis.bioRxiv : the preprint server for biology · 2025Article
- Article
- Biosynthesis of peptidic thiooxazole metallophores installed by multinuclear nonheme iron enzymes.bioRxiv : the preprint server for biology · 2025Article
- Co-opting the bacterial lipoprotein pathway in the biosynthesis of a lipidated macrocyclic peptide.bioRxiv : the preprint server for biology · 2025Article
- Phylogenomic Identification of a Highly Conserved Copper-Binding RiPP Biosynthetic Gene Cluster in MarineACS chemical biology · 2025Article
- The mechanism of thioamide formation by the YcfA-YcfC system in 6-thioguanine biosynthesis.Nature communications · 2025Article
- Multinuclear non-haem iron-dependent oxidative enzymes: landscape of their substrates, partner proteins and biosynthetic gene clusters.Microbial genomics · 2025Article
- Copper-chelating natural products.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2025Review
- Biosynthesis of unique natural product scaffolds by Fe(II)/αKG-dependent oxygenases.Journal of natural medicines · 2025Review
- A widespread family of ribosomal peptide metallophores involved in bacterial adaptation to metal stress.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Methanobactins: Structures, Biosynthesis, and Microbial Diversity.Annual review of microbiology · 2024Review
- Decarboxylation in Natural Products Biosynthesis.JACS Au · 2024Review
- A multi-iron enzyme installs copper-binding oxazolone/thioamide pairs on a nontypeableProceedings of the National Academy of Sciences of the United States of America · 2024Article
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Authors and funding
22 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Methanobactins (Mbns) are a family of copper-binding peptides involved in copper uptake by methanotrophs, and are potential therapeutic agents for treating diseases characterized by disordered copper accumulation. Mbns are produced via modification of MbnA precursor peptides at cysteine residues catalyzed by the core biosynthetic machinery containing MbnB, an iron-dependent enzyme, and MbnC. However, mechanistic details underlying the catalysis of the MbnBC holoenzyme remain unclear. Here, we present crystal structures of MbnABC complexes from two distinct species, revealing that the leader peptide of the substrate MbnA binds MbnC for recruitment of the MbnBC holoenzyme, while the core peptide of MbnA resides in the catalytic cavity created by the MbnB-MbnC interaction which harbors a unique tri-iron cluster. Ligation of the substrate sulfhydryl group to the tri-iron center achieves a dioxygen-dependent reaction for oxazolone-thioamide installation. Structural analysis of the MbnABC complexes together with functional investigation of MbnB variants identified a conserved catalytic aspartate residue as a general base required for MbnBC-mediated MbnA modification. Together, our study reveals the similar architecture and function of MbnBC complexes from different species, demonstrating an evolutionarily conserved catalytic mechanism of the MbnBC holoenzymes.
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