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Structure paper

TitlePlant receptor-like protein activation by a microbial glycoside hydrolase.
Journal, issue, pagesNature, Vol. 610, Issue 7931, Page 335-342, Year 2022
Publish dateSep 21, 2022
AuthorsYue Sun / Yan Wang / Xiaoxiao Zhang / Zhaodan Chen / Yeqiang Xia / Lei Wang / Yujing Sun / Mingmei Zhang / Yu Xiao / Zhifu Han / Yuanchao Wang / Jijie Chai /
PubMed AbstractPlants rely on cell-surface-localized pattern recognition receptors to detect pathogen- or host-derived danger signals and trigger an immune response. Receptor-like proteins (RLPs) with a leucine- ...Plants rely on cell-surface-localized pattern recognition receptors to detect pathogen- or host-derived danger signals and trigger an immune response. Receptor-like proteins (RLPs) with a leucine-rich repeat (LRR) ectodomain constitute a subgroup of pattern recognition receptors and play a critical role in plant immunity. Mechanisms underlying ligand recognition and activation of LRR-RLPs remain elusive. Here we report a crystal structure of the LRR-RLP RXEG1 from Nicotiana benthamiana that recognizes XEG1 xyloglucanase from the pathogen Phytophthora sojae. The structure reveals that specific XEG1 recognition is predominantly mediated by an amino-terminal and a carboxy-terminal loop-out region (RXEG1(ID)) of RXEG1. The two loops bind to the active-site groove of XEG1, inhibiting its enzymatic activity and suppressing Phytophthora infection of N. benthamiana. Binding of XEG1 promotes association of RXEG1(LRR) with the LRR-type co-receptor BAK1 through RXEG1(ID) and the last four conserved LRRs to trigger RXEG1-mediated immune responses. Comparison of the structures of apo-RXEG1(LRR), XEG1-RXEG1(LRR) and XEG1-BAK1-RXEG1(LRR) shows that binding of XEG1 induces conformational changes in the N-terminal region of RXEG1(ID) and enhances structural flexibility of the BAK1-associating regions of RXEG1(LRR). These changes allow fold switching of RXEG1(ID) for recruitment of BAK1(LRR). Our data reveal a conserved mechanism of ligand-induced heterodimerization of an LRR-RLP with BAK1 and suggest a dual function for the LRR-RLP in plant immunity.
External linksNature / PubMed:36131021
MethodsEM (single particle) / X-ray diffraction
Resolution2.92 - 3.59 Å
Structure data

30826

7drc

EMDB-30826, PDB-7drc:
Cryo-EM structure of plant receptor like protein RXEG1 in complex with xyloglucanase XEG1 and BAK1
Method: EM (single particle) / Resolution: 2.92 Å

32293

7w3t

EMDB-32293, PDB-7w3t:
Cryo-EM structure of plant receptor like kinase NbBAK1 in RXEG1-BAK1-XEG1 complex
Method: EM (single particle) / Resolution: 3.59 Å

32294

7w3v

EMDB-32294, PDB-7w3v:
Plant receptor like protein RXEG1 in complex with xyloglucanase XEG1
Method: EM (single particle) / Resolution: 3.11 Å

32295

7w3x

EMDB-32295, PDB-7w3x:
Cryo-EM structure of plant receptor like protein RXEG1
Method: EM (single particle) / Resolution: 3.21 Å

PDB-7drb:
Crystal structure of plant receptor like protein RXEG1 with xyloglucanase XEG1
Method: X-RAY DIFFRACTION / Resolution: 3.3 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

Source
  • phytophthora sojae (eukaryote)
  • nicotiana benthamiana (plant)
KeywordsPLANT PROTEIN / LRR / PTI / Glycoside hydrolase / Inhibitor

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