7DEK

Pseudomonas aeruginosa FK506-binding protein PaFkbA

7DEK の概要

• エントリーDOI: 10.2210/pdb7dek/pdb
• 分子名称: Peptidyl-prolyl cis-trans isomerase (2 entities in total)
• 機能のキーワード: dimer, chaperone, isomerase
• 由来する生物種: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 89493.24

構造登録者

Ynag, J.,Huang, Q.,Bao, R. (登録日: 2020-11-04, 公開日: 2021-09-08, 最終更新日: 2023-11-29)

主引用文献

Huang, Q.,Yang, J.,Li, C.,Song, Y.,Zhu, Y.,Zhao, N.,Mou, X.,Tang, X.,Luo, G.,Tong, A.,Sun, B.,Tang, H.,Li, H.,Bai, L.,Bao, R.
Structural characterization of PaFkbA: A periplasmic chaperone from Pseudomonas aeruginosa .
Comput Struct Biotechnol J, 19:2460-2467, 2021

PubMed Abstract: Bacterial Mip-like FK506-binding proteins (FKBPs) mostly exhibit peptidyl-prolyl-cis/-isomerase (PPIase) and chaperone activities. These activities are associated with various intracellular functions with diverse molecular mechanisms. Herein, we report the gene-encoded crystal structure of the 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 MucD.

PubMed: 34025936
DOI: 10.1016/j.csbj.2021.04.045

実験手法

X-RAY DIFFRACTION (2.9 Å)