8GPP

Acinetobacter baumannii carbonic anhydrase PaaY

8GPP の概要

• エントリーDOI: 10.2210/pdb8gpp/pdb
• 分子名称: Carbonic anhydrase, BICARBONATE ION, ZINC ION, ... (5 entities in total)
• 機能のキーワード: acinetobacter baumannii, carbonic anhydrase, trimer, carbohydrate
• 由来する生物種: Acinetobacter baumannii
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 68767.77

構造登録者

Wen, Y.,Jiao, M. (登録日: 2022-08-26, 公開日: 2023-05-31, 最終更新日: 2025-02-26)

主引用文献

Jiao, M.,He, W.,Ouyang, Z.,Qin, Q.,Guo, Y.,Zhang, J.,Bai, Y.,Guo, X.,Yu, Q.,She, J.,Hwang, P.M.,Zheng, F.,Wen, Y.
Mechanistic and structural insights into the bifunctional enzyme PaaY from Acinetobacter baumannii.
Structure, 31:935-947.e4, 2023

PubMed Abstract: PaaY is a thioesterase that enables toxic metabolites to be degraded through the bacterial phenylacetic acid (PA) pathway. The Acinetobacter baumannii gene FQU82_01591 encodes PaaY, which we demonstrate to possess γ-carbonic anhydrase activity in addition to thioesterase activity. The crystal structure of AbPaaY in complex with bicarbonate reveals a homotrimer with a canonical γ-carbonic anhydrase active site. Thioesterase activity assays demonstrate a preference for lauroyl-CoA as a substrate. The AbPaaY trimer structure shows a unique domain-swapped C-termini, which increases the stability of the enzyme in vitro and decreases its susceptibility to proteolysis in vivo. The domain-swapped C-termini impact thioesterase substrate specificity and enzyme efficacy without affecting carbonic anhydrase activity. AbPaaY knockout reduced the growth of Acinetobacter in media containing PA, decreased biofilm formation, and impaired hydrogen peroxide resistance. Collectively, AbPaaY is a bifunctional enzyme that plays a key role in the metabolism, growth, and stress response mechanisms of A. baumannii.

PubMed: 37329879
DOI: 10.1016/j.str.2023.05.015

実験手法

X-RAY DIFFRACTION (2.09 Å)