8GPM

Acinetobacter baumannii carbonic anhydrase

Summary for 8GPM

• Entry DOI: 10.2210/pdb8gpm/pdb
• Descriptor: Carbonic anhydrase, GLYCEROL, ZINC ION, ... (5 entities in total)
• Functional Keywords: acinetobacter baumannii, carbonic anhydrase, trimer, carbohydrate
• Biological source: Acinetobacter baumannii
• Total number of polymer chains: 1
• Total formula weight: 22094.45

Authors

Wen, Y.,Jiao, M. (deposition date: 2022-08-26, release date: 2023-05-31, Last modification date: 2025-02-26)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.7 Å)