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2.4.1.264: D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphoundecaprenol 2-beta-glucuronosyltransferase

This is an abbreviated version!
For detailed information about D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphoundecaprenol 2-beta-glucuronosyltransferase, go to the full flat file.

Reaction

UDP-alpha-D-glucuronate
+
alpha-D-Man-(1->3)-beta-D-Glc-(1->4)-alpha-D-Glc-1-diphospho-ditrans,octacis-undecaprenol
=
UDP
+
beta-D-GlcA-(1->2)-alpha-D-Man-(1->3)-beta-D-Glc-(1->4)-alpha-D-Glc-1-diphospho-ditrans,octacis-undecaprenol

Synonyms

gumK

ECTree

     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.264 D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphoundecaprenol 2-beta-glucuronosyltransferase

Crystallization

Crystallization on EC 2.4.1.264 - D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphoundecaprenol 2-beta-glucuronosyltransferase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method, crystal structure of apo-enzyme at 1.9 A resolution, and of enzyme in complex with UDP, at 2.28 A resolution. Residue Asp157 serves as the general base in the transfer reaction. Residues M231, M273, E272, Y292, M306, K307, and Q310 interact with UDP. Cocrystallisation of GumK or mutant D157A in presence of UDP-glucuronate is not possible
hanging-drop vapour diffusion method, crystals of recombinant GumK, 1.9 A resolution
-
in silico-built models of GumK complexed with UDP-GlcA as well as its analogs UDP-glucose and UDP-galacturonic acid. UDP-GlcA binding to GumK triggers a change in the GumK tertiary structure, affecting N-terminal hydrophobic residues to generate or improve the lipid-derived acceptor substrate site, while UDP-GlcA accommodates the transfer reaction