9FYC

The barley MLA13-AVRA13 heterodimer

Summary for 9FYC

• Entry DOI: 10.2210/pdb9fyc/pdb
• EMDB information: 50863
• Descriptor: CC-NBS-LRR resistance protein MLA13, CSEP0372 putative effector protein (2 entities in total)
• Functional Keywords: complex, apoptosis, immune receptor, mildew, antifungal protein
• Biological source: Hordeum vulgare; More
• Total number of polymer chains: 2
• Total formula weight: 121826.68

Authors

Behrmann, E.,Schulze-Lefert, P.,Flores-Ibarra, A.,Lawson, A.W. (deposition date: 2024-07-03, release date: 2025-02-12, Last modification date: 2025-06-11)

Primary citation

Lawson, A.W.,Flores-Ibarra, A.,Cao, Y.,An, C.,Neumann, U.,Gunkel, M.,Saur, I.M.L.,Chai, J.,Behrmann, E.,Schulze-Lefert, P.
The barley MLA13-AVR A13 heterodimer reveals principles for immunoreceptor recognition of RNase-like powdery mildew effectors.
Embo J., 44:3210-3230, 2025

PubMed Abstract: Co-evolution between cereals and pathogenic grass powdery mildew fungi is exemplified by sequence diversification of an allelic series of barley resistance genes encoding Mildew Locus A (MLA) nucleotide-binding leucine-rich repeat (NLR) immunoreceptors with an N-terminal coiled-coil domain (CNLs). Each immunoreceptor recognises a matching, strain-specific powdery mildew effector encoded by an avirulence gene (AVR). We present here the cryo-EM structure of barley MLA13 in complex with its cognate effector AVR-1. The effector adopts an RNase-like fold when bound to MLA13 in planta, similar to crystal structures of other RNase-like AVR effectors unbound to receptors. AVR-1 interacts via its basal loops with MLA13 C-terminal leucine-rich repeats (LRRs) and the central winged helix domain (WHD). Co-expression of structure-guided MLA13 and AVR-1 substitution variants show that the receptor-effector interface plays an essential role in mediating immunity-associated plant cell death. Furthermore, by combining structural information from the MLA13-AVR-1 heterocomplex with sequence alignments of other MLA receptors, we engineered a single amino acid substitution in MLA7 that enables expanded effector detection of AVR-1 and the virulent variant AVR-V2. In contrast to the pentameric conformation of previously reported effector-activated CNL resistosomes, MLA13 was purified and resolved as a stable heterodimer from an in planta expression system. Our study suggests a common structural principle for RNase-like effector binding to MLAs and highlights the utility of structure-guided engineering of plant immune receptors for broadening their pathogen effector recognition capabilities.

PubMed: 39948409
DOI: 10.1038/s44318-025-00373-9

Experimental method

ELECTRON MICROSCOPY (3.8 Å)