2J42
low quality crystal structure of the transport component C2-II of the C2-toxin from Clostridium botulinum
Summary for 2J42
| Entry DOI | 10.2210/pdb2j42/pdb |
| Descriptor | C2 TOXIN COMPONENT-II (1 entity in total) |
| Functional Keywords | toxin, clostridium botulinum, c2-ii |
| Biological source | CLOSTRIDIUM BOTULINUM |
| Total number of polymer chains | 1 |
| Total formula weight | 80766.56 |
| Authors | Schleberger, C.,Hochmann, H.,Barth, H.,Aktories, K.,Schulz, G.E. (deposition date: 2006-08-24, release date: 2006-10-11, Last modification date: 2023-12-13) |
| Primary citation | 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 Cited by 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: 17027031DOI: 10.1016/J.JMB.2006.09.002 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.13 Å) |
Structure validation
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