6H3P

Crystal structure of the cytoplasmic chorismate mutase from Zea mays

6H3P の概要

• エントリーDOI: 10.2210/pdb6h3p/pdb
• 分子名称: Chorismate mutase (2 entities in total)
• 機能のキーワード: chorismate mutase, zea mays, plant protein
• 由来する生物種: Zea mays
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 56754.84

構造登録者

Altegoer, F.,Bange, G. (登録日: 2018-07-19, 公開日: 2019-01-16, 最終更新日: 2024-01-17)

主引用文献

Han, X.,Altegoer, F.,Steinchen, W.,Binnebesel, L.,Schuhmacher, J.,Glatter, T.,Giammarinaro, P.I.,Djamei, A.,Rensing, S.A.,Reissmann, S.,Kahmann, R.,Bange, G.
A kiwellin disarms the metabolic activity of a secreted fungal virulence factor.
Nature, 565:650-653, 2019

PubMed Abstract: Fungi-induced plant diseases affect global food security and plant ecology. The biotrophic fungus Ustilago maydis causes smut disease in maize (Zea mays) plants by secreting numerous virulence effectors that reprogram plant metabolism and immune responses. The secreted fungal chorismate mutase Cmu1 presumably affects biosynthesis of the plant immune signal salicylic acid by channelling chorismate into the phenylpropanoid pathway. Here we show that one of the 20 maize-encoded kiwellins (ZmKWL1) specifically blocks the catalytic activity of Cmu1. ZmKWL1 hinders substrate access to the active site of Cmu1 through intimate interactions involving structural features that are specific to fungal Cmu1 orthologues. Phylogenetic analysis suggests that plant kiwellins have a versatile scaffold that can specifically counteract pathogen effectors such as Cmu1. We reveal the biological activity of a member of the kiwellin family, a widely conserved group of proteins that have previously been recognized only as important human allergens.

PubMed: 30651637
DOI: 10.1038/s41586-018-0857-9

実験手法

X-RAY DIFFRACTION (2.7 Å)