PMID:19761218
| Citation |
Sheng, F, Yep, A, Feng, L, Preiss, J and Geiger, JH (2009) Oligosaccharide binding in Escherichia coli glycogen synthase. Biochemistry 48:10089-97 |
|---|---|
| Abstract |
Glycogen/starch synthase elongates glucan chains and is the key enzyme in the synthesis of glycogen in bacteria and starch in plants. Cocrystallization of Escherichia coli wild-type glycogen synthase (GS) with substrate ADPGlc and the glucan acceptor mimic HEPPSO produced a closed form of GS and suggests that domain-domain closure accompanies glycogen synthesis. Cocrystallization of the inactive GS mutant E377A with substrate ADPGlc and oligosaccharide results in the first oligosaccharide-bound glycogen synthase structure. Four bound oligosaccharides are observed, one in the interdomain cleft (G6a) and three on the N-terminal domain surface (G6b, G6c, and G6d). Extending from the center of the enzyme to the interdomain cleft opening, G6a mostly interacts with the highly conserved N-terminal domain residues lining the cleft of GS. The surface-bound oligosaccharides G6c and G6d have less interaction with enzyme and exhibit a more curled, helixlike structural arrangement. The observation that oligosaccharides bind only to the N-terminal domain of GS suggests that glycogen in vivo probably binds to only one side of the enzyme to ensure unencumbered interdomain movement, which is required for efficient, continuous glucan-chain synthesis. |
| Links |
PubMed Online version:10.1021/bi900916t |
| Keywords |
Amino Acid Sequence; Binding Sites; Catalysis; Crystallography, X-Ray; Escherichia coli/enzymology; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/metabolism; Glycogen Synthase/chemistry; Glycogen Synthase/metabolism; Molecular Sequence Data; Oligosaccharides/chemistry; Oligosaccharides/metabolism; Substrate Specificity |
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