8IKX
An Arabidopsis polygalacturonase PGLR
8IKX の概要
| エントリーDOI | 10.2210/pdb8ikx/pdb |
| 分子名称 | Pectin lyase-like superfamily protein, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total) |
| 機能のキーワード | polygalacturonase, hydrolase |
| 由来する生物種 | Arabidopsis thaliana (thale cress) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 42989.05 |
| 構造登録者 | |
| 主引用文献 | 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 Cited by 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: 38359129DOI: 10.1126/science.adj9529 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.5 Å) |
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