5ZF2

Crystal structure of Trxlp from Edwardsiella tarda EIB202

5ZF2 の概要

• エントリーDOI: 10.2210/pdb5zf2/pdb
• 分子名称: Thioredoxin (H-type,TRX-H), SULFATE ION (3 entities in total)
• 機能のキーワード: thioredoxin-like protein, t4ss effector, ask1-mapk signaling cascades., oxidoreductase
• 由来する生物種: Edwardsiella tarda (strain EIB202)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11718.07

構造登録者

Yang, C.,Quan, S. (登録日: 2018-03-02, 公開日: 2019-03-06, 最終更新日: 2023-11-22)

主引用文献

Yang, D.,Liu, X.,Xu, W.,Gu, Z.,Yang, C.,Zhang, L.,Tan, J.,Zheng, X.,Wang, Z.,Quan, S.,Zhang, Y.,Liu, Q.
The Edwardsiella piscicida thioredoxin-like protein inhibits ASK1-MAPKs signaling cascades to promote pathogenesis during infection.
Plos Pathog., 15:e1007917-e1007917, 2019

PubMed Abstract: It is important that bacterium can coordinately deliver several effectors into host cells to disturb the cellular progress during infection, however, the precise role of effectors in host cell cytosol remains to be resolved. In this study, we identified a new bacterial virulence effector from pathogenic Edwardsiella piscicida, which presents conserved crystal structure to thioredoxin family members and is defined as a thioredoxin-like protein (Trxlp). Unlike the classical bacterial thioredoxins, Trxlp can be translocated into host cells, mimicking endogenous thioredoxin to abrogate ASK1 homophilic interaction and phosphorylation, then suppressing the phosphorylation of downstream Erk1/2- and p38-MAPK signaling cascades. Moreover, Trxlp-mediated inhibition of ASK1-Erk/p38-MAPK axis promotes the pathogenesis of E. piscicida in zebrafish larvae infection model. Taken together, these data provide insights into the mechanism underlying the bacterial thioredoxin as a virulence effector in downmodulating the innate immune responses during E. piscicida infection.

PubMed: 31314784
DOI: 10.1371/journal.ppat.1007917

実験手法

X-RAY DIFFRACTION (1.98 Å)