1UKF

Crystal Structure of Pseudomonas Avirulence Protein AvrPphB

1UKF の概要

• エントリーDOI: 10.2210/pdb1ukf/pdb
• 分子名称: Avirulence protein AVRPPH3 (2 entities in total)
• 機能のキーワード: avrpphb, avrpph3, avirulence, hypersensitive response, hydrolase
• 由来する生物種: Pseudomonas syringae pv. phaseolicola
• 細胞内の位置: Secreted: Q52430
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20387.29

構造登録者

Zhu, M.,Shao, F.,Innes, R.W.,Dixon, J.E.,Xu, Z. (登録日: 2003-08-21, 公開日: 2003-12-09, 最終更新日: 2023-12-27)

主引用文献

Zhu, M.,Shao, F.,Innes, R.W.,Dixon, J.E.,Xu, Z.
The crystal structure of Pseudomonas avirulence protein AvrPphB: a papain-like fold with a distinct substrate-binding site.
Proc.Natl.Acad.Sci.Usa, 101:302-307, 2004

PubMed Abstract: AvrPphB is an avirulence (Avr) protein from the plant pathogen Pseudomonas syringae that can trigger a disease-resistance response in a number of host plants including Arabidopsis. AvrPphB belongs to a novel family of cysteine proteases with the charter member of this family being the Yersinia effector protein YopT. AvrPphB has a very stringent substrate specificity, catalyzing a single proteolytic cleavage in the Arabidopsis serine/threonine kinase PBS1. We have determined the crystal structure of AvrPphB by x-ray crystallography at 1.35-A resolution. The structure is composed of a central antiparallel beta-sheet, with alpha-helices packing on both sides of the sheet to form a two-lobe structure. The core of this structure resembles the papain-like cysteine proteases. The similarity includes the AvrPphB active site catalytic triad of Cys-98, His-212, and Asp-227 and the oxyanion hole residue Asn-93. Based on analogy with inhibitor complexes of the papain-like proteases, we propose a model for the substrate-binding mechanism of AvrPphB. A deep and positively charged pocket (S2) and a neighboring shallow surface (S3) likely bind to aspartic acid and glycine residues in the substrate located two (P2) and three (P3) residues N terminal to the cleavage site, respectively. Further implications about the specificity of plant pathogen recognition are also discussed.

PubMed: 14694194
DOI: 10.1073/pnas.2036536100

実験手法

X-RAY DIFFRACTION (1.35 Å)