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8BDW

Crystal structure of CnaB2 domain from Lactobacillus plantarum

Summary for 8BDW
Entry DOI10.2210/pdb8bdw/pdb
DescriptorCell surface adherence protein,collagen-binding domain, LPXTG-motif cell wall anchor, GLYCEROL, SULFATE ION, ... (5 entities in total)
Functional Keywordscnab domain, isopeptide bond, catcher/tag pair, protein ligation, peptide binding protein
Biological sourceLactiplantibacillus plantarum
Total number of polymer chains12
Total formula weight123350.45
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 citationFan, 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: 36695475
DOI: 10.1002/anie.202216371
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.86 Å)
Structure validation

227111

數據於2024-11-06公開中

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