9CCQ の概要
| エントリーDOI | 10.2210/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: 40153490DOI: 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) |
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