1R5E

Solution structure of the folded core of Pseudomonas syringae effector protein, AvrPto

1R5E の概要

• エントリーDOI: 10.2210/pdb1r5e/pdb
• 分子名称: avirulence protein (1 entity in total)
• 機能のキーワード: three-helix bundle, omega loop, protein binding
• 由来する生物種: Pseudomonas syringae
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13117.42

構造登録者

Wulf, J.,Pascuzzi, P.E.,Martin, G.B.,Nicholson, L.K. (登録日: 2003-10-10, 公開日: 2004-10-19, 最終更新日: 2024-05-22)

主引用文献

Wulf, J.,Pascuzzi, P.E.,Fahmy, A.,Martin, G.B.,Nicholson, L.K.
The solution structure of type III effector protein AvrPto reveals conformational and dynamic features important for plant pathogenesis.
STRUCTURE, 12:1257-1268, 2004

PubMed Abstract: Pseudomonas syringae pv. tomato, the causative agent of bacterial speck disease of tomato, uses a type III secretion system (TTSS) to deliver effector proteins into the host cell. In resistant plants, the bacterial effector protein AvrPto physically interacts with the host Pto kinase and elicits antibacterial defense responses. In susceptible plants, which lack the Pto kinase, AvrPto acts as a virulence factor to promote bacterial growth. The solution structure of AvrPto reveals a functional core consisting of a three-helix bundle motif flanked by disordered N- and C-terminal tails. Residues required for Pto binding lie in a 19 residue Omega loop. Modeling suggests a hydrophobic patch involving the activation loop of Pto forms a contact surface with the AvrPto Omega loop and that helix packing mediates interactions between AvrPto and putative virulence targets Api2 and Api3. The AvrPto structure has a low stability that may facilitate chaperone-independent secretion by the TTSS.

PubMed: 15242602
DOI: 10.1016/j.str.2004.04.017

実験手法

SOLUTION NMR