8BDW
Crystal structure of CnaB2 domain from Lactobacillus plantarum
Summary for 8BDW
Entry DOI | 10.2210/pdb8bdw/pdb |
Descriptor | Cell surface adherence protein,collagen-binding domain, LPXTG-motif cell wall anchor, GLYCEROL, SULFATE ION, ... (5 entities in total) |
Functional Keywords | cnab domain, isopeptide bond, catcher/tag pair, protein ligation, peptide binding protein |
Biological source | Lactiplantibacillus plantarum |
Total number of polymer chains | 12 |
Total formula weight | 123350.45 |
Authors | Taberman, H.,Hakanpaa, J.,Linder, M.B.,Aranko, A.S. (deposition date: 2022-10-20, release date: 2023-02-22, Last modification date: 2024-10-23) |
Primary citation | Fan, R.,Hakanpaa, J.,Elfving, K.,Taberman, H.,Linder, M.B.,Aranko, A.S. Biomolecular Click Reactions Using a Minimal pH-Activated Catcher/Tag Pair for Producing Native-Sized Spider-Silk Proteins. Angew.Chem.Int.Ed.Engl., 62:e202216371-e202216371, 2023 Cited by PubMed Abstract: A type of protein/peptide pair known as Catcher/Tag pair spontaneously forms an intermolecular isopeptide bond which can be applied for biomolecular click reactions. Covalent protein conjugation using Catcher/Tag pairs has turned out to be a valuable tool in biotechnology and biomedicines, but it is essential to increase the current toolbox of orthogonal Catcher/Tag pairs to expand the range of applications further, for example, for controlled multiple-fragment ligation. We report here the engineering of novel Catcher/Tag pairs for protein ligation, aided by a crystal structure of a minimal CnaB domain from Lactobacillus plantarum. We show that a newly engineered pair, called SilkCatcher/Tag enables efficient pH-inducible protein ligation in addition to being compatible with the widely used SpyCatcher/Tag pair. Finally, we demonstrate the use of the SilkCatcher/Tag pair in the production of native-sized highly repetitive spider-silk-like proteins with >90 % purity, which is not possible by traditional recombinant production methods. PubMed: 36695475DOI: 10.1002/anie.202216371 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.86 Å) |
Structure validation
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