2J3V

Crystal structure of the enzymatic component C2-I of the C2-toxin from Clostridium botulinum at pH 3.0

2J3V の概要

• エントリーDOI: 10.2210/pdb2j3v/pdb
• 関連するPDBエントリー: 2J3X 2J3Z
• 分子名称: C2 TOXIN COMPONENT I, GLYCEROL, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: adp-ribosyltransferase, toxin, clostridium botulinum
• 由来する生物種: CLOSTRIDIUM BOTULINUM
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 52088.85

構造登録者

Schleberger, C.,Hochmann, H.,Barth, H.,Aktories, K.,Schulz, G.E. (登録日: 2006-08-23, 公開日: 2006-10-11, 最終更新日: 2024-05-08)

主引用文献

Schleberger, C.,Hochmann, H.,Barth, H.,Aktories, K.,Schulz, G.E.
Structure and Action of the Binary C2 Toxin from Clostridium Botulinum.
J.Mol.Biol., 364:705-, 2006

PubMed Abstract: C2 toxin from Clostridium botulinum is composed of the enzyme component C2-I, which ADP-ribosylates actin, and the binding and translocation component C2-II, responsible for the interaction with eukaryotic cell receptors and the following endocytosis. Three C2-I crystal structures at resolutions of up to 1.75 A are presented together with a crystal structure of C2-II at an appreciably lower resolution and a model of the prepore formed by fragment C2-IIa. The C2-I structure was determined at pH 3.0 and at pH 6.1. The structural differences are small, indicating that C2-I does not unfold, even at a pH value as low as 3.0. The ADP-ribosyl transferase activity of C2-I was determined for alpha and beta/gamma-actin and related to that of Iota toxin and of mutant S361R of C2-I that introduced the arginine observed in Iota toxin. The substantial activity differences between alpha and beta/gamma-actin cannot be explained by the protein structures currently available. The structure of the transport component C2-II at pH 4.3 was established by molecular replacement using a model of the protective antigen of anthrax toxin at pH 6.0. The C-terminal receptor-binding domain of C2-II could not be located but was present in the crystals. It may be mobile. The relative orientation and positions of the four other domains of C2-II do not differ much from those of the protective antigen, indicating that no large conformational changes occur between pH 4.3 and pH 6.0. A model of the C2-IIa prepore structure was constructed based on the corresponding assembly of the protective antigen. It revealed a surprisingly large number of asparagine residues lining the pore. The interaction between C2-I and C2-IIa and the translocation of C2-I into the target cell are discussed.

PubMed: 17027031
DOI: 10.1016/J.JMB.2006.09.002

実験手法

X-RAY DIFFRACTION (2.11 Å)