8IKW

A complex structure of PGIP-PG

Summary for 8IKW

• Entry DOI: 10.2210/pdb8ikw/pdb
• Descriptor: Polygalacturonase inhibitor 2, Endo-polygalacturonase, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total)
• Functional Keywords: pgip, polygalacturonase, hydrolase
• Biological source: Phaseolus vulgaris; More
• Total number of polymer chains: 8
• Total formula weight: 287165.06

Authors

Xiao, Y.,Chai, J. (deposition date: 2023-03-01, release date: 2024-02-07, Last modification date: 2024-10-16)

Primary citation

Xiao, Y.,Sun, G.,Yu, Q.,Gao, T.,Zhu, Q.,Wang, R.,Huang, S.,Han, Z.,Cervone, F.,Yin, H.,Qi, T.,Wang, Y.,Chai, J.
A plant mechanism of hijacking pathogen virulence factors to trigger innate immunity.
Science, 383:732-739, 2024

PubMed Abstract: Polygalacturonase-inhibiting proteins (PGIPs) interact with pathogen-derived polygalacturonases to inhibit their virulence-associated plant cell wall-degrading activity but stimulate immunity-inducing oligogalacturonide production. Here we show that interaction between PGIP2 (PvPGIP2) and polygalacturonase (FpPG) enhances substrate binding, resulting in inhibition of the enzyme activity of FpPG. This interaction promotes FpPG-catalyzed production of long-chain immunoactive oligogalacturonides, while diminishing immunosuppressive short oligogalacturonides. PvPGIP2 binding creates a substrate binding site on PvPGIP2-FpPG, forming a new polygalacturonase with boosted substrate binding activity and altered substrate preference. Structure-based engineering converts a putative PGIP that initially lacks FpPG-binding activity into an effective FpPG-interacting protein. These findings unveil a mechanism for plants to transform pathogen virulence activity into a defense trigger and provide proof of principle for engineering PGIPs with broader specificity.

PubMed: 38359129
DOI: 10.1126/science.adj9529

Experimental method

X-RAY DIFFRACTION (1.94 Å)