6Q1X
Lasso peptide pandonodin
Summary for 6Q1X
| Entry DOI | 10.2210/pdb6q1x/pdb |
| NMR Information | BMRB: 30651 |
| Descriptor | Pandonodin (1 entity in total) |
| Functional Keywords | lasso peptide, ripps, unknown function |
| Biological source | Pandoraea norimbergensis |
| Total number of polymer chains | 1 |
| Total formula weight | 3330.96 |
| Authors | Link, A.J.,Cheung-Lee, W.L. (deposition date: 2019-08-06, release date: 2019-12-04, Last modification date: 2024-05-15) |
| Primary citation | Cheung-Lee, W.L.,Cao, L.,Link, A.J. Pandonodin: A Proteobacterial Lasso Peptide with an Exceptionally Long C-Terminal Tail. Acs Chem.Biol., 14:2783-2792, 2019 Cited by PubMed Abstract: Lasso peptides are a family of ribosomally synthesized and post-translationally modified peptides (RiPPs) defined by their threaded-ring topology. The N-terminus of the peptide forms an isopeptide bond with an aspartate or glutamate side chain to create a 7-9 amino acid (aa) macrocyclic ring through which the rest of the peptide is threaded. The result is a highly constrained three-dimensional structure. Even though they share a threaded-ring feature, characterized lasso peptides vary greatly in sequence and size, ranging from 14 to 26 aa. Using genome mining, we identified a new lasso peptide gene cluster with a predicted lasso peptide that is 33 aa long. Here we report the heterologous expression of this new peptide, pandonodin, its NMR structure, and its unusual biophysical properties. Pandonodin has a long, proteolytically resistant 18-residue tail of low sequence complexity, which limits its water solubility. Within this tail is a 6 aa disulfide-bonded macrocycle that serves as a steric lock to maintain the lasso structure. This disulfide bond is unusually stable, requiring both heat and high concentrations of reductants for cleavage. Finally, we also show that segments of the C-terminal tail of pandonodin can be replaced with arbitrary sequences, allowing for the construction of pandonodin-protein fusions. PubMed: 31742991DOI: 10.1021/acschembio.9b00676 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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