8V1J

Structure of an allelic variant of Puccinia graminis f. sp. tritici (Pgt) effector AvrSr27 (AvrSr27-1)

8V1J の概要

• エントリーDOI: 10.2210/pdb8v1j/pdb
• 分子名称: AvrSr27, ZINC ION (3 entities in total)
• 機能のキーワード: fungal effector protein, metal binding protein
• 由来する生物種: Puccinia graminis f. sp. tritici
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 27511.81

構造登録者

Outram, M.A.,Williams, S.J.,Ericsson, D.J. (登録日: 2023-11-20, 公開日: 2024-06-12, 最終更新日: 2024-06-19)

主引用文献

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

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: 38730532
DOI: 10.1111/nph.19801

実験手法

X-RAY DIFFRACTION (2.41596376588 Å)