9KAR
Solution NMR structure of a new lasso peptide streptacidin
Summary for 9KAR
| Entry DOI | 10.2210/pdb9kar/pdb |
| Descriptor | GLY-GLY-TRP-GLY-THR-VAL-PRO-ASP-TRP-PHE-PHE-ASN-MET-ASN-TRP (1 entity in total) |
| Functional Keywords | lasso peptide, topological structure, solution nmr structure, ripps, antibiotic |
| Biological source | Streptacidiphilus jiangxiensis |
| Total number of polymer chains | 1 |
| Total formula weight | 1813.99 |
| Authors | |
| Primary citation | Huang, J.,Cheng, B.,Cao, C.,Liu, W. Genome mining and heterologous expression reveal streptacidin, a new lasso peptide from Streptacidiphilus jiangxiensis. Org.Biomol.Chem., 23:1723-1730, 2025 Cited by PubMed Abstract: A lasso peptide biosynthetic gene cluster (BGC) was identified through genome mining in the species CGMCC 4.1857, which was isolated from acidic rhizosphere soil. The BGC was reconstructed in , leading to the heterologous production of a lasso peptide named streptacidin. The solution structure of streptacidin was determined based on the distance constraints derived from the NOESY spectrum, establishing the first lasso peptide utilizing methionine as a steric lock for the unique spatial configuration and the remarkable stability against heat (up to 95 °C) and proteolytic degradation by carboxypeptidase Y and chymotrypsin. Under experimental conditions, streptacidin showed weak effectiveness against vancomycin sensitive ATCC 29212 and ATCC 902. These findings further the understanding of this distinctive class of compounds. PubMed: 39807060DOI: 10.1039/d4ob01998a PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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