Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Escherichia coli |
Crystallization (Comment) | Organism |
---|---|
structure of the wild-type enzyme bound to ADP and glucose reveals a 15.2° overall domain-domain closure. The main chain carbonyl group of His-161, Arg-300, and Lys-305 are suggested to act as critical catalytic residues in the transglycosylation. Glu-377 is found on the-face of the glucose and plays an electrostatic role in the active site and as a glucose ring locator. In the mutant E377A-ADP-4-(2-hydroxyethyl)piperazine-1-(2-hydroxypropane)sulfonic acid complex the glucose moiety is either absent or disordered in the active site | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
C7S/C409S | exhibits comparable specific activity and apparent affinity for ADP-Glc to wild-type. Use as alternative in crystallization trials to avoid aggregation | Escherichia coli |
E377A | crystallization data, in the mutant E377A-ADP-4-(2-hydroxyethyl)piperazine-1-(2-hydroxypropane)sulfonic acid complex the glucose moiety is either absent or disordered in the active site | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P0A6U8 | - |
- |
Synonyms | Comment | Organism |
---|---|---|
glycogen synthase | - |
Escherichia coli |