2bvm

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Image:2bvm.gif

2bvm, resolution 2.55Å

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CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF TOXIN B FROM CLOSTRIDIUM DIFFICILE IN COMPLEX WITH UDP, GLC AND MANGANESE ION

Overview

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.

About this Structure

2BVM is a Single protein structure of sequence from Clostridium difficile with , , and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Structural basis for the function of Clostridium difficile toxin B., Reinert DJ, Jank T, Aktories K, Schulz GE, J Mol Biol. 2005 Sep 2;351(5):973-81. PMID:16054646

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