The biosynthesis of methanobactin

Metal homeostasis poses a major challenge to microbes, which must acquire scarce elements for core metabolic processes. Methanobactin, an extensively modified copper-chelating peptide, was one of the earliest natural products shown to enable microbial acquisition of a metal other than iron. We descr...

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Bibliographic Details
Published in:	Science (American Association for the Advancement of Science) 2018-03, Vol.359 (6382), p.1411-1416
Main Authors:	Kenney, Grace E, Dassama, Laura M K, Pandelia, Maria-Eirini, Gizzi, Anthony S, Martinie, Ryan J, Gao, Peng, DeHart, Caroline J, Schachner, Luis F, Skinner, Owen S, Ro, Soo Y, Zhu, Xiao, Sadek, Monica, Thomas, Paul M, Almo, Steven C, Bollinger, Jr, J Martin, Krebs, Carsten, Kelleher, Neil L, Rosenzweig, Amy C
Format:	Article
Language:	eng
Subjects:	Amino Acid Sequence Biosynthesis Carbon sources Chelation Copper Copper - metabolism Enzymes Genome, Bacterial Genomes Heavy metals Homeostasis Homology Imidazoles - chemistry Imidazoles - metabolism Iron Ligands Machinery Metals Methane Methylosinus trichosporium - genetics Methylosinus trichosporium - metabolism Microorganisms Microprocessors Natural products Oligopeptides - biosynthesis Oligopeptides - chemistry Oligopeptides - genetics Oligopeptides - metabolism Oxazolone Oxidation Oxidation-Reduction Oxygen - metabolism Peptides Precursors Protein Conformation, alpha-Helical Protein Multimerization Protein Processing, Post-Translational
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Summary:	Metal homeostasis poses a major challenge to microbes, which must acquire scarce elements for core metabolic processes. Methanobactin, an extensively modified copper-chelating peptide, was one of the earliest natural products shown to enable microbial acquisition of a metal other than iron. We describe the core biosynthetic machinery responsible for the characteristic posttranslational modifications that grant methanobactin its specificity and affinity for copper. A heterodimer comprising MbnB, a DUF692 family iron enzyme, and MbnC, a protein from a previously unknown family, performs a dioxygen-dependent four-electron oxidation of the precursor peptide (MbnA) to install an oxazolone and an adjacent thioamide, the characteristic methanobactin bidentate copper ligands. MbnB and MbnC homologs are encoded together and separately in many bacterial genomes, suggesting functions beyond their roles in methanobactin biosynthesis.
ISSN:	0036-8075 1095-9203