Cloned (Comment) | Organism |
---|---|
- |
Escherichia coli |
Crystallization (Comment) | Organism |
---|---|
protein is a tetramer with 222 point group symmetry. Each subunit is dominated by an eight-stranded mixed beta-sheet with two additional layers of beta-sheets and ten alpha-helices. Q109 and D137 anchor the uracil ring and the ribose of UDP-glucose to the protein.The beta-phosphoryl group of the product lies close to the epsilon-nitrogen of K202, the carboxylate group of E201 can bridge the 2- and 3-hydroxyl groups of the glucosyl moiety | Escherichia coli |
to 1.9 A resolution. Modeling of UDP-glucose into the active site. The side chains of Gln109 and Asp137, respectively, serve to anchor the uracil ring and the ribose of UDP-glucose to the protein. The beta-phosphoryl group of the product is predicted to lie within hydrogen bonding distance to the eosilon-nitrogen of Lys202 whereas the carboxylate group of Glu201 is predicted to bridge the 2'- and 3'-hydroxyl groups of the glucosyl moiety | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P0AEP3 | - |
- |
Subunits | Comment | Organism |
---|---|---|
tetramer | crystallization data | Escherichia coli |