5NO9

NLPPya in complex with mannosamine

5NO9 の概要

• エントリーDOI: 10.2210/pdb5no9/pdb
• 関連するPDBエントリー: 5NNW
• 分子名称: 25 kDa protein elicitor, MAGNESIUM ION, 2-amino-2-deoxy-alpha-D-mannopyranose, ... (4 entities in total)
• 機能のキーワード: actinoporin-like proteins, nep1-like proteins, complex with hexose, toxin
• 由来する生物種: Pythium aphanidermatum
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 96807.54

構造登録者

Podobnik, M.,Anderluh, G.,Lenarcic, T. (登録日: 2017-04-11, 公開日: 2017-12-27, 最終更新日: 2024-11-06)

主引用文献

Lenarcic, T.,Albert, I.,Bohm, H.,Hodnik, V.,Pirc, K.,Zavec, A.B.,Podobnik, M.,Pahovnik, D.,Zagar, E.,Pruitt, R.,Greimel, P.,Yamaji-Hasegawa, A.,Kobayashi, T.,Zienkiewicz, A.,Gomann, J.,Mortimer, J.C.,Fang, L.,Mamode-Cassim, A.,Deleu, M.,Lins, L.,Oecking, C.,Feussner, I.,Mongrand, S.,Anderluh, G.,Nurnberger, T.
Eudicot plant-specific sphingolipids determine host selectivity of microbial NLP cytolysins.
Science, 358:1431-1434, 2017

PubMed Abstract: Necrosis and ethylene-inducing peptide 1-like (NLP) proteins constitute a superfamily of proteins produced by plant pathogenic bacteria, fungi, and oomycetes. Many NLPs are cytotoxins that facilitate microbial infection of eudicot, but not of monocot plants. Here, we report glycosylinositol phosphorylceramide (GIPC) sphingolipids as NLP toxin receptors. Plant mutants with altered GIPC composition were more resistant to NLP toxins. Binding studies and x-ray crystallography showed that NLPs form complexes with terminal monomeric hexose moieties of GIPCs that result in conformational changes within the toxin. Insensitivity to NLP cytolysins of monocot plants may be explained by the length of the GIPC head group and the architecture of the NLP sugar-binding site. We unveil early steps in NLP cytolysin action that determine plant clade-specific toxin selectivity.

PubMed: 29242345
DOI: 10.1126/science.aan6874

実験手法

X-RAY DIFFRACTION (1.75 Å)