7BW5
a new lasso peptide koreensin
Summary for 7BW5
| Entry DOI | 10.2210/pdb7bw5/pdb |
| NMR Information | BMRB: 36343 |
| Descriptor | lasso peptide koreensin (1 entity in total) |
| Functional Keywords | lasso peptide, unknown function |
| Biological source | Sphingomonas koreensis |
| Total number of polymer chains | 1 |
| Total formula weight | 1672.84 |
| Authors | Hemmi, H.,Kodani, S. (deposition date: 2020-04-13, release date: 2020-09-09, Last modification date: 2024-05-15) |
| Primary citation | Fuwa, H.,Hemmi, H.,Kaweewan, I.,Kozaki, I.,Honda, H.,Kodani, S. Heterologous production of new lasso peptide koreensin based on genome mining. J Antibiot (Tokyo), 74:42-50, 2021 Cited by PubMed Abstract: Lasso peptides are a class of ribosomally biosynthesized and posttranslationally modified peptides with a knot structure as a common motif. Based on a genome search, a new biosynthetic gene cluster of lasso peptide was found in the genome of the proteobacterium Sphingomonas koreensis. Interestingly, the amino acid sequence of the precursor peptide gene includes two cell adhesion motif sequences (KGD and DGR). Heterologous production of the new lasso peptide was performed using the cryptic biosynthetic gene cluster of S. koreensis. As a result, a new lasso peptide named koreensin was produced by the gene expression system in the host strain Sphingomonas subterranea. The structure of koreensin was determined by NMR and ESI-MS analysis. The three-dimensional structure of koreensin was obtained based on an NOE experiment and the coupling constants. A variant peptide (koreensin-RGD), which had RGD instead of KGD, was produced by heterologous production with site-directed mutagenesis experiment. Koreensin and koreensin-RGD did not show cell adhesion inhibitory activity, although the molecules possessed cell adhesion motifs. The possible presence of a salt bridge between the motifs in koreensin was indicated, and it may prevent the cell adhesion motif from functioning. PubMed: 32855516DOI: 10.1038/s41429-020-00363-5 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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