4G6T

Structure of the HopA1-SchA Chaperone-Effector Complex

4G6T の概要

• エントリーDOI: 10.2210/pdb4g6t/pdb
• 分子名称: Type III chaperone protein ShcA, Type III effector HopA1 (3 entities in total)
• 機能のキーワード: chaperone effector, secretion chaperone, chaperone
• 由来する生物種: Pseudomonas syringae pv. tomato; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 23185.54

構造登録者

Stebbins, C.E.,Janjusevic, R.,Quezada, C.M. (登録日: 2012-07-19, 公開日: 2013-06-05, 最終更新日: 2024-02-28)

主引用文献

Janjusevic, R.,Quezada, C.M.,Small, J.,Stebbins, C.E.
Structure of the HopA1(21-102)-ShcA chaperone-effector complex of Pseudomonas syringae reveals conservation of a virulence factor binding motif from animal to plant pathogens.
J.Bacteriol., 195:658-664, 2013

PubMed Abstract: Pseudomonas syringae injects numerous bacterial proteins into host plant cells through a type 3 secretion system (T3SS). One of the first such bacterial effectors discovered, HopA1, is a protein that has unknown functions in the host cell but possesses close homologs that trigger the plant hypersensitive response in resistant strains. Like the virulence factors in many bacterial pathogens of animals, HopA1 depends upon a cognate chaperone in order to be effectively translocated by the P. syringae T3SS. Herein, we report the crystal structure of a complex of HopA1(21-102) with its chaperone, ShcA, determined to 1.56-Å resolution. The structure reveals that three key features of the chaperone-effector interactions found in animal pathogens are preserved in the Gram-negative pathogens of plants, namely, (i) the interaction of the chaperone with a nonglobular polypeptide of the effector, (ii) an interaction centered on the so-called β-motif, and (iii) the presence of a conserved hydrophobic patch in the chaperone that recognizes the β-motif. Structure-based mutagenesis and biochemical studies have established that the β-motif is critical for the stability of this complex. Overall, these results show that the β-motif interactions are broadly conserved in bacterial pathogens utilizing T3SSs, spanning an interkingdom host range.

PubMed: 23204470
DOI: 10.1128/JB.01621-12

実験手法

X-RAY DIFFRACTION (1.56 Å)