2M8F
Structure of lasso peptide astexin3
Summary for 2M8F
| Entry DOI | 10.2210/pdb2m8f/pdb |
| NMR Information | BMRB: 19250 |
| Descriptor | astexin3 (1 entity in total) |
| Functional Keywords | sidechain-to-backbone link, unknown function |
| Biological source | Asticcacaulis excentricus |
| Total number of polymer chains | 1 |
| Total formula weight | 2542.76 |
| Authors | Maksimov, M.O.,Link, A. (deposition date: 2013-05-18, release date: 2013-07-31, Last modification date: 2024-11-27) |
| Primary citation | Maksimov, M.O.,Link, A.J. Discovery and characterization of an isopeptidase that linearizes lasso peptides. J.Am.Chem.Soc., 135:12038-12047, 2013 Cited by PubMed Abstract: Lasso peptides are a class of ribosomally derived natural products with diverse bioactivities. The characteristic threaded lasso structure in these peptides derives from an isopeptide bond attaching the N-terminus of the peptide to an acidic side chain. Here we describe the heterologous expression of a lasso peptide gene cluster encoding two lasso peptides, astexin-2 and astexin-3, and solve the solution structure of astexin-3. This cluster also encodes an enzyme annotated as a protease. We show that this enzyme, AtxE2, is a lasso peptide isopeptidase that specifically hydrolyzes astexins-2 and -3, converting them to linear peptides. Astexin-3 is highly thermostable and resists unthreading after extensive heat treatment. In contrast, astexin-2 unthreads upon heat treatment. AtxE2 has no activity toward unthreaded astexin-2, demonstrating that this isopeptidase must recognize a knotted structure in order to function. We also use this isopeptidase as a tool to study evolutionary relationships between lasso peptide gene clusters. PubMed: 23862624DOI: 10.1021/ja4054256 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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