6AVY

Crystal structure of Zea mays acyl-protein thioesterase 2

6AVY の概要

• エントリーDOI: 10.2210/pdb6avy/pdb
• 分子名称: Acyl-protein thioesterase 2 (2 entities in total)
• 機能のキーワード: alpha/beta hydrolase, acyl-protein thioesterase, hydrolase
• 由来する生物種: Zea mays (Maize)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 54475.43

構造登録者

Burger, M.,Willige, B.C.,Chory, J. (登録日: 2017-09-04, 公開日: 2017-12-27, 最終更新日: 2023-10-04)

主引用文献

Burger, M.,Willige, B.C.,Chory, J.
A hydrophobic anchor mechanism defines a deacetylase family that suppresses host response against YopJ effectors.
Nat Commun, 8:2201-2201, 2017

PubMed Abstract: Several Pseudomonas and Xanthomonas species are plant pathogens that infect the model organism Arabidopsis thaliana and important crops such as Brassica. Resistant plants contain the infection by rapid cell death of the infected area through the hypersensitive response (HR). A family of highly related α/β hydrolases is involved in diverse processes in all domains of life. Functional details of their catalytic machinery, however, remained unclear. We report the crystal structures of α/β hydrolases representing two different clades of the family, including the protein SOBER1, which suppresses AvrBsT-incited HR in Arabidopsis. Our results reveal a unique hydrophobic anchor mechanism that defines a previously unknown family of protein deacetylases. Furthermore, this study identifies a lid-loop as general feature for substrate turnover in acyl-protein thioesterases and the described family of deacetylases. Furthermore, we found that SOBER1's biological function is not restricted to Arabidopsis thaliana and not limited to suppress HR induced by AvrBsT.

PubMed: 29259199
DOI: 10.1038/s41467-017-02347-w

実験手法

X-RAY DIFFRACTION (2.24 Å)