5T56
[3]catenane from MccJ25 G12R/I13C/G21C lasso peptide
Summary for 5T56
Entry DOI | 10.2210/pdb5t56/pdb |
NMR Information | BMRB: 30165 |
Descriptor | Microcin J25 (2 entities in total) |
Functional Keywords | catenane, lasso peptide, de novo protein |
Biological source | Escherichia coli More |
Cellular location | Secreted: Q9X2V7 Q9X2V7 |
Total number of polymer chains | 4 |
Total formula weight | 4561.16 |
Authors | Link, A.J.,Allen, C.D. (deposition date: 2016-08-30, release date: 2017-07-12, Last modification date: 2024-11-13) |
Primary citation | Allen, C.D.,Link, A.J. Self-Assembly of Catenanes from Lasso Peptides. J. Am. Chem. Soc., 138:14214-14217, 2016 Cited by PubMed Abstract: Lasso peptides exist naturally in a threaded state as [1]rotaxanes, and we reasoned that lasso peptides cleaved in their loop region could serve as building blocks for catenanes. Mutagenesis of the lasso peptide microcin J25 (MccJ25) with two cysteine residues followed by cleavage of the peptide with trypsin led to a [2]rotaxane structure that self-assembled into a [3]catenane and [4]catenanes at room temperature in aqueous solution. The [3]catenane represents the smallest ring size of a catenane composed solely of polypeptide segments. The NMR structure of the [3]catenane was determined, suggesting that burial of hydrophobic residues may be a driving force for assembly of the catenane structure. PubMed: 27768305DOI: 10.1021/jacs.6b09454 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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