5Z1V

Crystal structure of AvrPib

5Z1V の概要

• エントリーDOI: 10.2210/pdb5z1v/pdb
• 分子名称: AvrPib protein (2 entities in total)
• 機能のキーワード: magnaporthe oryzae, max effector, protein crystal structure, unknown function
• 由来する生物種: Magnaporthe oryzae (Rice blast fungus)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 29751.66

構造登録者

Zhang, X.,He, D.,Zhao, Y.X.,Taylor, I.A.,Peng, Y.L.,Yang, J.,Liu, J.F. (登録日: 2017-12-28, 公開日: 2018-09-05, 最終更新日: 2024-10-16)

主引用文献

Zhang, X.,He, D.,Zhao, Y.,Cheng, X.,Zhao, W.,Taylor, I.A.,Yang, J.,Liu, J.,Peng, Y.L.
A positive-charged patch and stabilized hydrophobic core are essential for avirulence function of AvrPib in the rice blast fungus.
Plant J., 96:133-146, 2018

PubMed Abstract: Fungal avirulence effectors, a key weapon utilized by pathogens to promote their infection, are recognized by immune receptors to boost host R gene-mediated resistance. Many avirulence effectors share sparse sequence homology to proteins with known functions, and their molecular and biochemical functions together with the evolutionary relationship among different members remain largely unknown. Here, the crystal structure of AvrPib, an avirulence effector from Magnaporthe oryzae, was determined and showed a high degree of similarity to the M. oryzae Avrs and ToxB (MAX) effectors. Compared with other MAX effectors, AvrPib has a distinct positive-charge patch formed by five positive-charged residues (K29, K30, R50, K52 and K70) on the surface. These five key residues were essential to avirulence function of AvrPib and affected its nuclear localization into host cells. Moreover, residues V39 and V58, which locate in the hydrophobic core of the structure, cause loss of function of AvrPib by single-point mutation in natural isolates. In comparison with the wild-type AvrPib, the V39A or V58A mutations resulted in a partial or entire loss of secondary structure elements. Taken together, our results suggest that differences in the surface charge distribution of avirulence proteins could be one of the major bases for the variation in effector-receptor specificity, and that destabilization of the hydrophobic core is one of the major mechanisms employed by AvrPib for the fungus to evade recognition by resistance factors in the host cell.

PubMed: 29989241
DOI: 10.1111/tpj.14023

実験手法

X-RAY DIFFRACTION (1.661 Å)