8G33

Activated form of a CDCL long protein

これはPDB形式変換不可エントリーです。

8G33 の概要

• エントリーDOI: 10.2210/pdb8g33/pdb
• 分子名称: Hemolysin (2 entities in total)
• 機能のキーワード: pore-forming toxin, cholesterol-dependent cytolysin like, elizabethkingia anophelis, toxin
• 由来する生物種: Elizabethkingia anophelis Ag1
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 55906.49

構造登録者

Johnstone, B.A.,Christie, M.P.,Morton, C.J.,Parker, M.W. (登録日: 2023-02-06, 公開日: 2024-02-07, 最終更新日: 2025-04-09)

主引用文献

Johnstone, B.A.,Christie, M.P.,Joseph, R.,Morton, C.J.,Brown, H.G.,Hanssen, E.,Sanford, T.C.,Abrahamsen, H.L.,Tweten, R.K.,Parker, M.W.
Structural basis for the pore-forming activity of a complement-like toxin.
Sci Adv, 11:eadt2127-eadt2127, 2025

PubMed Abstract: Pore-forming proteins comprise a highly diverse group of proteins exemplified by the membrane attack complex/perforin (MACPF), cholesterol-dependent cytolysin (CDC), and gasdermin superfamilies, which all form gigantic pores (>150 angstroms). A recently found family of pore-forming toxins, called CDC-like proteins (CDCLs), are wide-spread in gut microbes and are a prevalent means of antibacterial antagonism. However, the structural aspects of how CDCLs assemble a pore remain a mystery. Here, we report the crystal structure of a proteolytically activated CDCL and cryo-electron microscopy structures of a prepore-like intermediate and a transmembrane pore providing detailed snapshots across the entire pore-forming pathway. These studies reveal a sophisticated array of regulatory features to ensure productive pore formation, and, thus, CDCLs straddle the MACPF, CDC, and gasdermin lineages of the giant pore superfamilies.

PubMed: 40153490
DOI: 10.1126/sciadv.adt2127

実験手法

X-RAY DIFFRACTION (2.49 Å)