6Q40
A secreted LysM effector of the wheat pathogen Zymoseptoria tritici protects the fungal hyphae against chitinase hydrolysis through ligand-dependent polymerisation of LysM homodimers
6Q40 の概要
エントリーDOI | 10.2210/pdb6q40/pdb |
関連するBIRD辞書のPRD_ID | PRD_900017 |
分子名称 | LysM domain-containing protein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, CHLORIDE ION, ... (4 entities in total) |
機能のキーワード | lectin, chitine-binding, oligomerization, protomer, lysm, hydrolase |
由来する生物種 | Zymoseptoria tritici IPO323 |
タンパク質・核酸の鎖数 | 4 |
化学式量合計 | 35340.22 |
構造登録者 | Mesters, J.R.,Saleem-Batcha, R.,Sanchez-Vallet, A.,Thomma, B.P.H.J. (登録日: 2018-12-05, 公開日: 2019-10-16, 最終更新日: 2020-07-29) |
主引用文献 | Sanchez-Vallet, A.,Tian, H.,Rodriguez-Moreno, L.,Valkenburg, D.J.,Saleem-Batcha, R.,Wawra, S.,Kombrink, A.,Verhage, L.,de Jonge, R.,van Esse, H.P.,Zuccaro, A.,Croll, D.,Mesters, J.R.,Thomma, B.P.H.J. A secreted LysM effector protects fungal hyphae through chitin-dependent homodimer polymerization. Plos Pathog., 16:e1008652-e1008652, 2020 Cited by PubMed Abstract: Plants trigger immune responses upon recognition of fungal cell wall chitin, followed by the release of various antimicrobials, including chitinase enzymes that hydrolyze chitin. In turn, many fungal pathogens secrete LysM effectors that prevent chitin recognition by the host through scavenging of chitin oligomers. We previously showed that intrachain LysM dimerization of the Cladosporium fulvum effector Ecp6 confers an ultrahigh-affinity binding groove that competitively sequesters chitin oligomers from host immune receptors. Additionally, particular LysM effectors are found to protect fungal hyphae against chitinase hydrolysis during host colonization. However, the molecular basis for the protection of fungal cell walls against hydrolysis remained unclear. Here, we determined a crystal structure of the single LysM domain-containing effector Mg1LysM of the wheat pathogen Zymoseptoria tritici and reveal that Mg1LysM is involved in the formation of two kinds of dimers; a chitin-dependent dimer as well as a chitin-independent homodimer. In this manner, Mg1LysM gains the capacity to form a supramolecular structure by chitin-induced oligomerization of chitin-independent Mg1LysM homodimers, a property that confers protection to fungal cell walls against host chitinases. PubMed: 32574207DOI: 10.1371/journal.ppat.1008652 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.412 Å) |
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