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Literature summary for 2.4.1.21 extracted from

  • Sheng, F.; Jia, X.; Yep, A.; Preiss, J.; Geiger, J.H.
    The crystal structures of the open and catalytically competent closed conformation of Escherichia coli glycogen synthase (2009), J. Biol. Chem., 284, 17796-17807.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Escherichia coli

Crystallization (Commentary)

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

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

Organism UniProt Comment Textmining
Escherichia coli P0A6U8
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-

Synonyms

Synonyms Comment Organism
glycogen synthase
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Escherichia coli