Characterization of a Copper-Chelating Natural Product from the MethanotrophMethylosinussp. LW3

Yun Ji Park, Gerri M. Roberts, Rana Montaser, Grace E. Kenney, Paul M. Thomas, Neil L. Kelleher, Amy C. Rosenzweig*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

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 methanotrophMethylosinus(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 theMs. sp. LW3 Mbn operon content, providing support for the proposed role of an uncharacterized biosynthetic enzyme, MbnF, and expanding the diversity of known Mbns.

Original languageEnglish (US)
Pages (from-to)2845-2850
Number of pages6
JournalBiochemistry
Volume60
Issue number38
DOIs
StatePublished - Sep 28 2021

ASJC Scopus subject areas

  • Biochemistry

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