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EC Number Crystallization (Commentary)
Display the reaction diagram Show all sequences 2.4.1.264hanging 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
Display the reaction diagram Show all sequences 2.4.1.264hanging-drop vapour diffusion method, crystals of recombinant GumK, 1.9 A resolution
Display the reaction diagram Show all sequences 2.4.1.264in 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
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