2BVM

Crystal structure of the catalytic domain of toxin B from Clostridium difficile in complex with UDP, Glc and manganese ion

2BVM の概要

• エントリーDOI: 10.2210/pdb2bvm/pdb
• 関連するPDBエントリー: 2BVL
• 分子名称: TOXIN B, MANGANESE (II) ION, URIDINE-5'-DIPHOSPHATE, ... (6 entities in total)
• 機能のキーワード: toxin, glycosyltransferase
• 由来する生物種: CLOSTRIDIUM DIFFICILE
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 63659.70

構造登録者

Reinert, D.J.,Jank, T.,Aktories, K.,Schulz, G.E. (登録日: 2005-06-30, 公開日: 2005-08-03, 最終更新日: 2023-12-13)

主引用文献

Reinert, D.J.,Jank, T.,Aktories, K.,Schulz, G.E.
Structural Basis for the Function of Clostridium Difficile Toxin B.
J.Mol.Biol., 351:973-, 2005

PubMed Abstract: Toxin B is a member of the family of large clostridial cytotoxins which are of great medical importance. Its catalytic fragment was crystallized in the presence of UDP-glucose and Mn2+. The structure was determined at 2.2 A resolution, showing that toxin B belongs to the glycosyltransferase type A family. However, toxin B contains as many as 309 residues in addition to the common chainfold, which most likely contribute to the target specificity. A superposition with other glycosyltransferases shows the expected positions of the acceptor oxygen atom during glucosyl transfer and indicates further that the reaction proceeds probably along a single-displacement pathway. The C1'' donor carbon atom position is defined by the bound UDP and glucose. It assigns the surface area of toxin B that forms the interface to the target protein during the modifying reaction. A docking attempt brought the known acceptor atom, Thr37 O(gamma1) of the switch I region of the RhoA:GDP target structure, near the expected position. The relative orientation of the two proteins was consistent with both being attached to a membrane. Sequence comparisons between toxin B variants revealed that the highest exchange rate occurs around the active center at the putative docking interface, presumably due to a continuous hit-and-evasion struggle between Clostridia and their eukaryotic hosts.

PubMed: 16054646
DOI: 10.1016/J.JMB.2005.06.071

実験手法

X-RAY DIFFRACTION (2.55 Å)