Structural characterization of PaFkbA: A periplasmic chaperone from Pseudomonas aeruginosa

Structural characterization of PaFkbA: A periplasmic chaperone from Pseudomonas aeruginosa

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...

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Bibliographic Details
Main Authors: Qin Huang, Jing Yang, Changcheng Li, Yingjie Song, Yibo Zhu, Ninglin Zhao, Xingyu Mou, Xinyue Tang, Guihua Luo, Aiping Tong, Bo Sun, Hong Tang, Hong Li, Lang Bai, Rui Bao
Format: Article
Language:English
Published: Elsevier 2021-01-01
Series:Computational and Structural Biotechnology Journal
Subjects:
FKBP-type protein
Chaperone activity
Crystal structure
Inter-domain rearrangement
Pseudomonas aeruginosa
Online Access:http://www.sciencedirect.com/science/article/pii/S2001037021001574

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http://www.sciencedirect.com/science/article/pii/S2001037021001574

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