Structural characterization of PaFkbA: A periplasmic chaperone from Pseudomonas aeruginosa

Computational and Structural Biotechnology Journal

Rui Bao¹  Aiping Tong²  Yingjie Song²  Jing Yang²  Guihua Luo²  Ninglin Zhao²  Changcheng Li²  Bo Sun²  Hong Li²  Xingyu Mou²  Xinyue Tang²  Hong Tang²  Qin Huang²  Yibo Zhu²  Lang Bai³ 

[1] Center of Infectious Diseases, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University and Collaborative Innovation Center, Chengdu, China;Center of Infectious Diseases, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University and Collaborative Innovation Center, Chengdu, China;Corresponding authors.;

关键词: FKBP-type protein;    Chaperone activity;    Crystal structure;    Inter-domain rearrangement;    Pseudomonas aeruginosa;   

DOI  :  

来源: DOAJ

【 摘 要 】

Bacterial Mip-like FK506-binding proteins (FKBPs) mostly exhibit peptidyl–prolyl-cis/trans-isomerase (PPIase) and chaperone activities. These activities are associated with various intracellular functions with diverse molecular mechanisms. Herein, we report the PA3262 gene-encoded crystal structure of the Pseudomonas aeruginosa PAO1′s Mip-like protein PaFkbA. Biochemical characterization of PaFkbA demonstrated PaFkbA’s chaperone activity for periplasmic protein MucD, a negative regulator of alginate biosynthesis. Furthermore, structural analysis of PaFkbA was used to describe the key features of PaFkbA chaperone activity. The outcomes of this analysis showed that the hinge region in the connecting helix of PaFbkA leads to the crucial conformational state transition for PaFkbA activity. Besides, the N-terminal domains participated in dimerization, and revealed its potential connection with FKBP domain and substrate binding. Mutagenesis and chaperone activity assay supported the theory that inter-domain motions are essential for PaFkbA function. These results provide biochemical and structural insights into the mechanism for FKBP’s chaperone activity and establish a plausible correlation between PaFkbA and P. aeruginosa MucD.

【 授权许可】

Unknown