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2.4.1.B62: small GTPase glucosyltransferase

This is an abbreviated version!
For detailed information about small GTPase glucosyltransferase, go to the full flat file.

Word Map on EC 2.4.1.B62

Reaction

UDP-alpha-D-glucose
+
a small GTPase
=
UDP
+
D-glucosyl-[a small GTPase]

Synonyms

Clostridium sordellii lethal toxin, cytotoxin B, cytotoxin L, glucosyltransferase TcdA, glucosyltransferase TcdB, haemorrhagic toxin, hemorrhagic toxin, letal toxin, lethal toxin, lethal-toxin, TcdA, TcdB, TcsH, TcsL, toxA, ToxB, toxin, toxin A, toxin B

ECTree

     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.B62 small GTPase glucosyltransferase

Crystallization

Crystallization on EC 2.4.1.B62 - small GTPase glucosyltransferase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
catalytic fragment of toxin B in the presence of UDP-glucose and Mn2+, to 2.2 A resolution. Toxin B belongs to the glycosyltransferase type A family. The reaction proceeds probably along a single-displacement pathway. The C1'' donor carbon atom position is defined by the bound UDP and glucose. The relative orientation of toxin B and substrate RhoA is consistent with both being attached to a membrane
crystal structures of the toxin A glucosyltransferase domain in the presence and absence of the co-substrate UDP-alpha-D-glucose, to 2.2 and 2.6 A resolution, respectively
enzyme contains an internal cysteine protease domain allosterically regulated by the eukaryotic-specific molecule inositol hexakisphosphate. Apo-cysteine protease is in dynamic equilibrium between active and inactive states. Inositol hexakisphosphate dramatically shifts this equilibrium towards an active conformer that is further restrained upon binding a suicide substrate. Residues within a beta-hairpin region functionally couple the inositol hexakisphosphate binding site to the active site
catalytic fragment, residues 1-551 to 2.85 A resolution. Geometry suggests that the reaction runs as a circular electron transfer in a six-membered ring, which involves the deprotonation of the nucleophile by the beta-phosphoryl group of the donor substrate UDP-glucose
catalytic fragment, residues 1-546, to 2.3 A resolution. Geometry suggests that the reaction runs as a circular electron transfer in a six-membered ring, which involves the deprotonation of the nucleophile by the beta-phosphoryl group of the donor substrate UDP-glucose