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9CCQ

Cryo-EM structure of the prepore-like EaCDCL short oligomer

これはPDB形式変換不可エントリーです。
9CCQ の概要
エントリーDOI10.2210/pdb9ccq/pdb
関連するPDBエントリー6XD4 8G32 8G33
EMDBエントリー45453
分子名称Thiol-activated cytolysin family protein, CALCIUM ION (2 entities in total)
機能のキーワードpore-forming toxin, cholesterol-dependent cytolysin like, elizabethkingia anophelis, macpf, complement, toxin
由来する生物種Elizabethkingia anophelis Ag1
タンパク質・核酸の鎖数30
化学式量合計1186023.75
構造登録者
Johnstone, B.A.,Christie, M.P.,Morton, C.M.,Brown, H.G.,Hanssen, E.,Parker, M.W. (登録日: 2024-06-23, 公開日: 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
Cited by
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
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (3.13 Å)
構造検証レポート
Validation report summary of 9ccq
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-02-04に公開中

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