8HZW
The NMR structure of noursinH11W peptide
Summary for 8HZW
| Entry DOI | 10.2210/pdb8hzw/pdb |
| Descriptor | noursinH11W (1 entity in total) |
| Functional Keywords | cyclic peptide, histidine-to-butyrine crosslink, histidinobutyrine, unknown function |
| Biological source | Streptomyces noursei ATCC 11455 |
| Total number of polymer chains | 1 |
| Total formula weight | 1669.97 |
| Authors | |
| Primary citation | Li, Y.,Ma, Y.,Xia, Y.,Zhang, T.,Sun, S.,Gao, J.,Yao, H.,Wang, H. Discovery and biosynthesis of tricyclic copper-binding ribosomal peptides containing histidine-to-butyrine crosslinks. Nat Commun, 14:2944-2944, 2023 Cited by PubMed Abstract: Cyclic peptide natural products represent an important class of bioactive compounds and clinical drugs. Enzymatic side-chain macrocyclization of ribosomal peptides is a major strategy developed by nature to generate these chemotypes, as exemplified by the superfamily of ribosomally synthesized and post-translational modified peptides. Despite the diverse types of side-chain crosslinks in this superfamily, the participation of histidine residues is rare. Herein, we report the discovery and biosynthesis of bacteria-derived tricyclic lanthipeptide noursin, which is constrained by a tri amino acid labionin crosslink and an unprecedented histidine-to-butyrine crosslink, named histidinobutyrine. Noursin displays copper-binding ability that requires the histidinobutyrine crosslink and represents the first copper-binding lanthipeptide. A subgroup of lanthipeptide synthetases, named LanKC, were identified to catalyze the formation of both the labionin and the histidinobutyrine crosslinks in precursor peptides and produce noursin-like compounds. The discovery of the histidinobutyrine-containing lanthipeptides expands the scope of post-translational modifications, structural diversity and bioactivity of ribosomally synthesized and post-translational modified peptides. PubMed: 37221219DOI: 10.1038/s41467-023-38517-2 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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