8BV0
Binary complex between the NB-ARC domain from the Tomato immune receptor NRC1 and the SPRY domain-containing effector SS15 from the potato cyst nematode
Summary for 8BV0
| Entry DOI | 10.2210/pdb8bv0/pdb |
| Descriptor | NRC1, Truncated secreted SPRY domain-containing protein 15 (Fragment), ADENOSINE-5'-DIPHOSPHATE (3 entities in total) |
| Functional Keywords | nlr, inhibitor, effector, sprysec, nematode, protein binding |
| Biological source | Solanum lycopersicum (tomato) More |
| Total number of polymer chains | 4 |
| Total formula weight | 130179.46 |
| Authors | Contreras, M.P.,Pai, H.,Muniyandi, S.,Toghani, A.,Lawson, D.M.,Tumtas, Y.,Duggan, C.,Yuen, E.L.H.,Stevenson, C.E.M.,Harant, A.,Wu, C.H.,Bozkurt, T.O.,Kamoun, S.,Derevnina, L. (deposition date: 2022-12-01, release date: 2022-12-21, Last modification date: 2024-06-19) |
| Primary citation | Contreras, M.P.,Pai, H.,Selvaraj, M.,Toghani, A.,Lawson, D.M.,Tumtas, Y.,Duggan, C.,Yuen, E.L.H.,Stevenson, C.E.M.,Harant, A.,Maqbool, A.,Wu, C.H.,Bozkurt, T.O.,Kamoun, S.,Derevnina, L. Resurrection of plant disease resistance proteins via helper NLR bioengineering. Sci Adv, 9:eadg3861-eadg3861, 2023 Cited by PubMed Abstract: Parasites counteract host immunity by suppressing helper nucleotide binding and leucine-rich repeat (NLR) proteins that function as central nodes in immune receptor networks. Understanding the mechanisms of immunosuppression can lead to strategies for bioengineering disease resistance. Here, we show that a cyst nematode virulence effector binds and inhibits oligomerization of the helper NLR protein NRC2 by physically preventing intramolecular rearrangements required for activation. An amino acid polymorphism at the binding interface between NRC2 and the inhibitor is sufficient for this helper NLR to evade immune suppression, thereby restoring the activity of multiple disease resistance genes. This points to a potential strategy for resurrecting disease resistance in crop genomes. PubMed: 37134163DOI: 10.1126/sciadv.adg3861 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (4.5 Å) |
Structure validation
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