7ZWJ
Triculamin: an Unusual Lasso Peptide with Potent Anti-mycobacterial Activity
Summary for 7ZWJ
| Entry DOI | 10.2210/pdb7zwj/pdb |
| NMR Information | BMRB: 34734 |
| Descriptor | Triculamin (1 entity in total) |
| Functional Keywords | lasso peptide, streptomyces triculaminicus, antimicrobial protein |
| Biological source | Streptomyces triculaminicus |
| Total number of polymer chains | 1 |
| Total formula weight | 1733.03 |
| Authors | Pedersen, K.D.,Gotfredsen, C.H.,Torring, T.,Juhl, D.W. (deposition date: 2022-05-19, release date: 2022-07-13, Last modification date: 2024-06-19) |
| Primary citation | Andersen, F.D.,Pedersen, K.D.,Wilkens Juhl, D.,Mygind, T.,Chopin, P.,B Svenningsen, E.,Poulsen, T.B.,Braad Lund, M.,Schramm, A.,Gotfredsen, C.H.,Torring, T. Triculamin: An Unusual Lasso Peptide with Potent Antimycobacterial Activity. J.Nat.Prod., 85:1514-1521, 2022 Cited by PubMed Abstract: Lasso peptides are ribosomally synthesized and post-translationally modified peptides (RiPPs) produced by microorganisms. Here we show that the two natural products triculamin and alboverticillin, originally isolated in 1967 and 1958, respectively, with potent and specific activity against mycobacteria are in fact the same lasso peptide. We solved the structure using 2D NMR spectroscopy and expanded on the previously reported bioactivity. Through genome sequencing, we identify the responsible biosynthetic gene clusters, which curiously revealed that, unlike any known lasso peptides, their precursor peptides appear to have a follower instead of a leader peptide. PubMed: 35748039DOI: 10.1021/acs.jnatprod.2c00065 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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