9G8U

Structure of the LipA:LipB complex from Acinetobacter baumannii

9G8U の概要

• エントリーDOI: 10.2210/pdb9g8u/pdb
• 分子名称: Lactonizing lipase, Lipase chaperone, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: lipase, secretion system, bacterial infection, chaperone complex, protein-protein interaction, lipid binding, lipid binding protein
• 由来する生物種: Acinetobacter baumannii; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 68384.70

構造登録者

de Oliveira Silva, Y.R.,Contreras-Martel, C.,Rodrigues de Melo, R.,Zanphorlin, L.,Trindade, D.M.,Dessen, A. (登録日: 2024-07-24, 公開日: 2025-02-19, 最終更新日: 2025-03-19)

主引用文献

de Oliveira Silva, Y.R.,Contreras-Martel, C.,Rodrigues de Melo, R.,Zanphorlin, L.M.,Trindade, D.M.,Dessen, A.
Architecture of an embracing lipase-foldase complex of the type II secretion system of Acinetobacter baumannii.
Structure, 33:601-612.e4, 2025

PubMed Abstract: Acinetobacter baumannii is a major human pathogen responsible for a growing number of multi-antibiotic-resistant infections, and of critical priority for the World Health Organization (WHO). A. baumannii employs a type II secretion system (T2SS) to secrete toxins extracellularly to enable cytotoxicity and colonization. Lipase LipA, secreted by the A. baumannii T2SS, is required for virulence and fitness, and in the periplasm is maintained in an active state by its essential foldase, LipB. Here we report that LipA is able to recognize lipids of different chain lengths at extremes of pH and temperature, thanks to its stabilization by LipB through an extended, highly helical "embrace." A vast bioinformatic analysis indicates that LipB-like foldases are widespread over numerous proteobacteria, and thus the extended foldase architecture shown here could be widespread. These results provide new insight into A. baumannii's adaptability as a pathogen in different environments and could facilitate the development of novel antibacterials.

PubMed: 39904335
DOI: 10.1016/j.str.2024.12.022

実験手法

X-RAY DIFFRACTION (3.174 Å)