6SUQ
Crystal Structure of TcdB2-TccC3-TEV
Summary for 6SUQ
Entry DOI | 10.2210/pdb6suq/pdb |
Descriptor | TcdB2,TccC3,Genome polyprotein (1 entity in total) |
Functional Keywords | toxins, tc toxins, toxin |
Biological source | Photorhabdus luminescens More |
Total number of polymer chains | 1 |
Total formula weight | 272965.94 |
Authors | Roderer, D.,Schubert, E.,Sitsel, O.,Raunser, S. (deposition date: 2019-09-16, release date: 2019-12-04, Last modification date: 2024-01-24) |
Primary citation | Roderer, D.,Schubert, E.,Sitsel, O.,Raunser, S. Towards the application of Tc toxins as a universal protein translocation system. Nat Commun, 10:5263-5263, 2019 Cited by PubMed Abstract: Tc toxins are bacterial protein complexes that inject cytotoxic enzymes into target cells using a syringe-like mechanism. Tc toxins are composed of a membrane translocator and a cocoon that encapsulates a toxic enzyme. The toxic enzyme varies between Tc toxins from different species and is not conserved. Here, we investigate whether the toxic enzyme can be replaced by other small proteins of different origin and properties, namely Cdc42, herpes simplex virus ICP47, Arabidopsis thaliana iLOV, Escherichia coli DHFR, Ras-binding domain of CRAF kinase, and TEV protease. Using a combination of electron microscopy, X-ray crystallography and in vitro translocation assays, we demonstrate that it is possible to turn Tc toxins into customizable molecular syringes for delivering proteins of interest across membranes. We also infer the guidelines that protein cargos must obey in terms of size, charge, and fold in order to apply Tc toxins as a universal protein translocation system. PubMed: 31748551DOI: 10.1038/s41467-019-13253-8 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.7 Å) |
Structure validation
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