9RDC
Crystal structure of Phytophthora infestans effector AVRcap1b in complex with the ENTH domain of Nicotiana benthamiana NbTOL9a protein
Summary for 9RDC
| Entry DOI | 10.2210/pdb9rdc/pdb |
| Descriptor | RxLR effector protein PITG_16705, Target of myb protein 1 (2 entities in total) |
| Functional Keywords | plant pathology, vesicle trafficking, escrt, plant immunity, protein binding |
| Biological source | Phytophthora infestans (potato late blight agent) More |
| Total number of polymer chains | 4 |
| Total formula weight | 174912.29 |
| Authors | Contreras, M.P.,Madhuprakash, J.,Lawson, D.M.,Kamoun, S. (deposition date: 2025-06-02, release date: 2025-07-16, Last modification date: 2026-06-17) |
| Primary citation | Madhuprakash, J.,Toghani, A.,Pai, H.,Harvey, M.,Bentham, A.R.,Seager, B.A.,Yuen, E.L.H.,De la Concepcion, J.C.,Lawson, D.M.,Stevenson, C.E.M.,Vergara-Cruces, A.,Derevnina, L.,Bozkurt, T.O.,Banfield, M.J.,Kamoun, S.,Contreras, M.P. A potato late blight pathogen effector interacts with ENTH-domain protein TOL9a and an activated helper NLR to suppress immunity. Sci Adv, 12:eaea4500-eaea4500, 2026 Cited by PubMed Abstract: Pathogens counteract central nodes of NLR immune receptor networks to suppress immunity. However, the mechanisms by which pathogens hijack helper NLR pathways are poorly understood. We show that an effector from the late blight pathogen interacts with the host protein NbTOL9a and a helper NLR to suppress immunity. We solved the crystal structure of the RXLR-LWY effector AVRcap1b in complex with the ENTH domain of NbTOL9a. The structure revealed that, unlike other RXLR-LWY effectors, AVRcap1b has a previously unidentified L-shaped fold that defines a distinct structural family of effectors in the genus . We defined the AVRcap1b/NbTOL9a binding interface and designed effector mutants that do not bind NbTOL9a, impairing immune suppression. This suggests that ENTH binding is required for full virulence activity. Last, we show that AVRcap1b associates specifically with activated NbNRC2 independently of NbTOL9a binding. We propose a model in which the effector interconnects NbNRC2 with the NbTOL9a pathway. Our results illustrate a previously uncharacterized pathogen mechanism to hijack NLR pathways and suppress immunity. PubMed: 42247512DOI: 10.1126/sciadv.aea4500 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (4.1 Å) |
Structure validation
Download full validation report
