2bvm
From Proteopedia
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==Overview== | ==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, . | + | 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== | ==About this Structure== | ||
| - | 2BVM is a | + | 2BVM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_difficile Clostridium difficile] with GLC, MN, SO4 and UDP as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BVM OCA]. |
==Reference== | ==Reference== | ||
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[[Category: toxin]] | [[Category: toxin]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:24:36 2007'' |
Revision as of 12:19, 5 November 2007
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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 GLC, MN, SO4 and UDP as ligands. Structure known Active Site: AC1. 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
Page seeded by OCA on Mon Nov 5 14:24:36 2007
Categories: Clostridium difficile | Single protein | Aktories, K. | Jank, T. | Reinert, D.J. | Schulz, G.E. | GLC | MN | SO4 | UDP | Glycosyltransferase | Toxin
