Abstract
Methanobactins (Mbns) are a growing family of ribosomally produced, post-translationally modified natural products. Characteristic nitrogen-containing heterocycles and neighboring thioamides allow these compounds to bind copper with high affinity. Genome mining has enabled the identification of Mbn operons in bacterial genomes and the prediction of diverse Mbn structures from operon content and precursor peptide sequence. Here we report the characterization of Mbn from Methylosinus (Ms.) species (sp.) LW4. The peptide backbone is distinct from all previously characterized Mbns, and the post-translational modifications correspond precisely to those predicted on the basis of the Ms. sp. LW4 Mbn operon. Thus, prediction based on genome analysis combined with isolation and structural characterization represents a phylogenetic approach to finding diverse Mbns and elucidating their biosynthetic pathways.
Original language | English (US) |
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Pages (from-to) | 11124-11127 |
Number of pages | 4 |
Journal | Journal of the American Chemical Society |
Volume | 138 |
Issue number | 35 |
DOIs | |
State | Published - Sep 7 2016 |
Funding
IMSERC is supported by NIH grants 1S10OD012016-01/1S10RR019071-01A1, Northwestern University/the state of Illinois, the IIN and the NSF under NNCI-1542205. High-resolution mass spectral analyses were partially supported by the NRTDP (GM108569). Funding for this work was provided by the NSF (MCB0842366 to A.C.R.), the NIH (GM070473 and GM118035 to A.C.R., GM111097 to B.M.H., AT009143 and GM108569 to N.L.K., 5T32GM008382 to M.O.R.), and the AHA (14PRE20460104 to G.E.K.).
ASJC Scopus subject areas
- General Chemistry
- Biochemistry
- Catalysis
- Colloid and Surface Chemistry