5XMG

Crystal structure of PA3488 from Pseudomonas aeruginosa

5XMG の概要

• エントリーDOI: 10.2210/pdb5xmg/pdb
• 分子名称: Uncharacterized protein (1 entity in total)
• 機能のキーワード: immunity protein, immune system
• 由来する生物種: Pseudomonas aeruginosa
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 43370.00

構造登録者

She, Z.,Gao, Z.Q. (登録日: 2017-05-15, 公開日: 2018-05-16, 最終更新日: 2024-10-23)

主引用文献

Yang, X.Y.,Li, Z.Q.,Gao, Z.Q.,Wang, W.J.,Geng, Z.,Xu, J.H.,She, Z.,Dong, Y.H.
Structural and SAXS analysis of Tle5-Tli5 complex reveals a novel inhibition mechanism of H2-T6SS in Pseudomonas aeruginosa.
Protein Sci., 26:2083-2091, 2017

PubMed Abstract: Widely spread in Gram-negative bacteria, the type VI secretion system (T6SS) secretes many effector-immunity protein pairs to help the bacteria compete against other prokaryotic rivals, and infect their eukaryotic hosts. Tle5 and Tle5B are two phospholipase effector protein secreted by T6SS of Pseudomonas aeruginosa. They can facilitate the bacterial internalization process into human epithelial cells by interacting with Akt protein of the PI3K-Akt signal pathway. Tli5 and PA5086-5088 are cognate immunity proteins of Tle5 and Tle5B, respectively. They can interact with their cognate effector proteins to suppress their virulence. Here, we report the crystal structure of Tli5 at 2.8Å resolution and successfully fit it into the Small angle X-ray scattering (SAXS) model of the complete Tle5-Tli5 complex. We identified two important motifs in Tli5 through sequence and structural analysis. One is a conserved loop-β-hairpin motif that exists in the Tle5 immunity homologs, the other is a long and sharp α-α motif that directly interacts with Tle5 according to SAXS data. We also distinguished the structural features of Tle5 and Tle5B family immunity proteins. Together, our work provided insights into a novel inhibition mechanism that may enhance our understanding of phospholipase D family proteins.

PubMed: 28758353
DOI: 10.1002/pro.3246

実験手法

X-RAY DIFFRACTION (2.8 Å)