8V1J
Structure of an allelic variant of Puccinia graminis f. sp. tritici (Pgt) effector AvrSr27 (AvrSr27-1)
Summary for 8V1J
| Entry DOI | 10.2210/pdb8v1j/pdb |
| Descriptor | AvrSr27, ZINC ION (3 entities in total) |
| Functional Keywords | fungal effector protein, metal binding protein |
| Biological source | Puccinia graminis f. sp. tritici |
| Total number of polymer chains | 2 |
| Total formula weight | 27511.81 |
| Authors | Outram, M.A.,Williams, S.J.,Ericsson, D.J. (deposition date: 2023-11-20, release date: 2024-06-12, Last modification date: 2024-06-19) |
| Primary citation | Outram, M.A.,Chen, J.,Broderick, S.,Li, Z.,Aditya, S.,Tasneem, N.,Arndell, T.,Blundell, C.,Ericsson, D.J.,Figueroa, M.,Sperschneider, J.,Dodds, P.N.,Williams, S.J. AvrSr27 is a zinc-bound effector with a modular structure important for immune recognition. New Phytol., 243:314-329, 2024 Cited by PubMed Abstract: Effector proteins are central to the success of plant pathogens, while immunity in host plants is driven by receptor-mediated recognition of these effectors. Understanding the molecular details of effector-receptor interactions is key for the engineering of novel immune receptors. Here, we experimentally determined the crystal structure of the Puccinia graminis f. sp. tritici (Pgt) effector AvrSr27, which was not accurately predicted using AlphaFold2. We characterised the role of the conserved cysteine residues in AvrSr27 using in vitro biochemical assays and examined Sr27-mediated recognition using transient expression in Nicotiana spp. and wheat protoplasts. The AvrSr27 structure contains a novel β-strand rich modular fold consisting of two structurally similar domains that bind to Zn ions. The N-terminal domain of AvrSr27 is sufficient for interaction with Sr27 and triggering cell death. We identified two Pgt proteins structurally related to AvrSr27 but with low sequence identity that can also associate with Sr27, albeit more weakly. Though only the full-length proteins, trigger Sr27-dependent cell death in transient expression systems. Collectively, our findings have important implications for utilising protein prediction platforms for effector proteins, and those embarking on bespoke engineering of immunity receptors as solutions to plant disease. PubMed: 38730532DOI: 10.1111/nph.19801 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.41596376588 Å) |
Structure validation
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