Characterization of a Copper-Chelating Natural Product from the Methanotroph Methylosinus sp. LW3
| Autor: | Rana Montaser, Grace E. Kenney, Neil L. Kelleher, Paul M. Thomas, Yun Ji Park, Amy C. Rosenzweig, Gerri M. Roberts |
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| Rok vydání: | 2021 |
| Předmět: |
Methanotroph
Operon Stereochemistry Gene Expression Biochemistry Article Oxazolone chemistry.chemical_compound Bacterial Proteins Amino Acid Sequence Thioamide Chelating Agents Methylosinus chemistry.chemical_classification Biological Products biology Imidazoles Gene Expression Regulation Bacterial biology.organism_classification Methylosinus trichosporium chemistry Anaerobic oxidation of methane Peptides Methane Oligopeptides Oxidation-Reduction Copper Genome Bacterial Bacteria Cysteine |
| Zdroj: | Biochemistry |
| ISSN: | 1520-4995 0006-2960 |
| DOI: | 10.1021/acs.biochem.1c00443 |
| Popis: | Methanobactins (Mbns) are ribosomally produced, post-translationally modified peptidic natural products that bind copper with high affinity. Methanotrophic bacteria use Mbns to acquire copper needed for enzymatic methane oxidation. Despite the presence of Mbn operons in a range of methanotroph and other bacterial genomes, few Mbns have been isolated and structurally characterized. Here we report the isolation of a novel Mbn from the methanotroph Methylosinus (Ms.) sp. LW3. Mass spectrometric and nuclear magnetic resonance spectroscopic data indicate that this Mbn, the largest characterized to date, consists of a 13-amino acid backbone modified to include pyrazinedione/oxazolone rings and neighboring thioamide groups derived from cysteine residues. The pyrazinedione ring is more stable to acid hydrolysis than the oxazolone ring and likely protects the Mbn from degradation. The structure corresponds exactly to that predicted on the basis of the Ms. sp. LW3 Mbn operon content, providing support for the proposed role of an uncharacterized biosynthetic enzyme, MbnF, and expanding the diversity of known Mbns. |
| Databáze: | OpenAIRE |
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