6IMP

Crystal structure of alpha-beta hydrolase (ABH) from Vibrio vulnificus

6IMP の概要

• エントリーDOI: 10.2210/pdb6imp/pdb
• 分子名称: RTX toxin RtxA (2 entities in total)
• 機能のキーワード: virulence, hydrolase, alpha-beta fold, toxins, toxin
• 由来する生物種: Vibrio vulnificus MO6-24/O
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 68912.70

構造登録者

Kim, M.H.,Hwang, J. (登録日: 2018-10-23, 公開日: 2019-08-21, 最終更新日: 2024-03-27)

主引用文献

Lee, Y.,Kim, B.S.,Choi, S.,Lee, E.Y.,Park, S.,Hwang, J.,Kwon, Y.,Hyun, J.,Lee, C.,Kim, J.F.,Eom, S.H.,Kim, M.H.
Makes caterpillars floppy-like effector-containing MARTX toxins require host ADP-ribosylation factor (ARF) proteins for systemic pathogenicity.
Proc.Natl.Acad.Sci.USA, 116:18031-18040, 2019

PubMed Abstract: Upon invading target cells, multifunctional autoprocessing repeats-in-toxin (MARTX) toxins secreted by bacterial pathogens release their disease-related modularly structured effector domains. However, it is unclear how a diverse repertoire of effector domains within these toxins are processed and activated. Here, we report that Makes caterpillars floppy-like effector (MCF)-containing MARTX toxins require ubiquitous ADP-ribosylation factor (ARF) proteins for processing and activation of intermediate effector modules, which localize in different subcellular compartments following limited processing of holo effector modules by the internal cysteine protease. Effector domains structured tandemly with MCF in intermediate modules become disengaged and fully activated by MCF, which aggressively interacts with ARF proteins present at the same location as intermediate modules and is converted allosterically into a catalytically competent protease. MCF-mediated effector processing leads ultimately to severe virulence in mice via an MCF-mediated ARF switching mechanism across subcellular compartments. This work provides insight into how bacteria take advantage of host systems to induce systemic pathogenicity.

PubMed: 31427506
DOI: 10.1073/pnas.1905095116

実験手法

X-RAY DIFFRACTION (2.62 Å)