8A14

Crystal structure of the cerato-platanin-like protein Cpl1 from Ustilago maydis

8A14 の概要

• エントリーDOI: 10.2210/pdb8a14/pdb
• 分子名称: Cerato-platatanin-like protein 1 (2 entities in total)
• 機能のキーワード: cerato-platatanin, double-psi-barrel, chitin-binding, sugar binding protein
• 由来する生物種: Ustilago maydis 521; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 220630.76

構造登録者

Weiland, P.,Bange, G.,Altegoer, F. (登録日: 2022-05-31, 公開日: 2023-05-17, 最終更新日: 2024-10-23)

主引用文献

Weiland, P.,Dempwolff, F.,Steinchen, W.,Freibert, S.A.,Tian, H.,Glatter, T.,Martin, R.,Thomma, B.P.H.J.,Bange, G.,Altegoer, F.
Structural and functional analysis of the cerato-platanin-like protein Cpl1 suggests diverging functions in smut fungi.
Mol Plant Pathol, 24:768-787, 2023

PubMed Abstract: Plant-pathogenic fungi are causative agents of the majority of plant diseases and can lead to severe crop loss in infected populations. Fungal colonization is achieved by combining different strategies, such as avoiding and counteracting the plant immune system and manipulating the host metabolome. Of major importance are virulence factors secreted by fungi, which fulfil diverse functions to support the infection process. Most of these proteins are highly specialized, with structural and biochemical information often absent. Here, we present the atomic structures of the cerato-platanin-like protein Cpl1 from Ustilago maydis and its homologue Uvi2 from Ustilago hordei. Both proteins adopt a double-Ψβ-barrel architecture reminiscent of cerato-platanin proteins, a class so far not described in smut fungi. Our structure-function analysis shows that Cpl1 binds to soluble chitin fragments via two extended grooves at the dimer interface of the two monomer molecules. This carbohydrate-binding mode has not been observed previously and expands the repertoire of chitin-binding proteins. Cpl1 localizes to the cell wall of U. maydis and might synergize with cell wall-degrading and decorating proteins during maize infection. The architecture of Cpl1 harbouring four surface-exposed loop regions supports the idea that it might play a role in the spatial coordination of these proteins. While deletion of cpl1 has only mild effects on the virulence of U. maydis, a recent study showed that deletion of uvi2 strongly impairs U. hordei virulence. Our structural comparison between Cpl1 and Uvi2 reveals sequence variations in the loop regions that might explain a diverging function.

PubMed: 37171083
DOI: 10.1111/mpp.13349

実験手法

X-RAY DIFFRACTION (1.9 Å)