9GCO
Xenorhabdus bovienii Thioredoxin complex with Rhs toxin TreX and immunity protein TriX
Summary for 9GCO
| Entry DOI | 10.2210/pdb9gco/pdb |
| Descriptor | Thioredoxin, Toxin TreX, Immunity Protein TriX, ... (6 entities in total) |
| Functional Keywords | adp-ribosyltransferase, toxin, thioredoxin |
| Biological source | Xenorhabdus bovienii SS-2004 More |
| Total number of polymer chains | 6 |
| Total formula weight | 89611.75 |
| Authors | Jurenas, D.,Terradot, L. (deposition date: 2024-08-02, release date: 2024-12-04, Last modification date: 2024-12-11) |
| Primary citation | Dumont, B.,Terradot, L.,Cascales, E.,Van Melderen, L.,Jurenas, D. Thioredoxin 1 moonlights as a chaperone for an interbacterial ADP-ribosyltransferase toxin. Nat Commun, 15:10388-10388, 2024 Cited by PubMed Abstract: Formation and breakage of disulfide bridges strongly impacts folding and activity of proteins. Thioredoxin 1 (TrxA) is a small, conserved enzyme that reduces disulfide bonds in the bacterial cytosol. In this study, we provide an example of the emergence of a chaperone role for TrxA, which is independent of redox catalysis. We show that the activity of the secreted bacterial ADP-ribosyltransferase (ART) toxin TreX, which does not contain any cysteines, is dependent on TrxA. TreX binds to the reduced form of TrxA via its carboxy-terminal extension to form a soluble and active complex. Structural studies revealed that TreX-like toxins are homologous to Scabin-like ART toxins which possess cysteine residues and form disulfide bridges at the position that superimposes the TrxA binding site in TreX. Our study therefore suggests that thioredoxin 1 evolved alternative functions by maintaining the interaction with cysteine-free substrates. PubMed: 39613764DOI: 10.1038/s41467-024-54892-w PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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