2bvm

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 4: Line 4:
==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, 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.
+
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==
Line 15: Line 15:
[[Category: Aktories, K.]]
[[Category: Aktories, K.]]
[[Category: Jank, T.]]
[[Category: Jank, T.]]
-
[[Category: Reinert, D.J.]]
+
[[Category: Reinert, D J.]]
-
[[Category: Schulz, G.E.]]
+
[[Category: Schulz, G E.]]
[[Category: GLC]]
[[Category: GLC]]
[[Category: MN]]
[[Category: MN]]
Line 24: Line 24:
[[Category: toxin]]
[[Category: toxin]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:28:18 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:42:06 2008''

Revision as of 14:42, 21 February 2008


2bvm, resolution 2.55Å

Drag the structure with the mouse to rotate

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

Page seeded by OCA on Thu Feb 21 16:42:06 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools