Oligosaccharide Binding in Escherichia coli Glycogen Synthase
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.
- Authors:
- Publication Date:
- Research Org.:
- Argonne National Lab. (ANL), Argonne, IL (United States)
- Sponsoring Org.:
- USDOE
- OSTI Identifier:
- 1006203
- Resource Type:
- Journal Article
- Journal Name:
- Biochemistry-US
- Additional Journal Information:
- Journal Volume: 48; Journal Issue: (42) ; 10, 2009; Journal ID: ISSN 0006-2960
- Country of Publication:
- United States
- Language:
- ENGLISH
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; 99 GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE; BACTERIA; CHAINS; CLOSURES; ENZYMES; ESCHERICHIA COLI; GLYCOGEN; IN VIVO; LINERS; MUTANTS; OLIGOSACCHARIDES; RESIDUES; STARCH; SUBSTRATES; SYNTHESIS
Citation Formats
Sheng, Fang, Yep, Alejandra, Feng, Lei, Preiss, Jack, Geiger, James H, and MSU). Oligosaccharide Binding in Escherichia coli Glycogen Synthase. United States: N. p., 2010.
Web. doi:10.1021/bi900916t.
Sheng, Fang, Yep, Alejandra, Feng, Lei, Preiss, Jack, Geiger, James H, & MSU). Oligosaccharide Binding in Escherichia coli Glycogen Synthase. United States. https://doi.org/10.1021/bi900916t
Sheng, Fang, Yep, Alejandra, Feng, Lei, Preiss, Jack, Geiger, James H, and MSU). 2010.
"Oligosaccharide Binding in Escherichia coli Glycogen Synthase". United States. https://doi.org/10.1021/bi900916t.
@article{osti_1006203,
title = {Oligosaccharide Binding in Escherichia coli Glycogen Synthase},
author = {Sheng, Fang and Yep, Alejandra and Feng, Lei and Preiss, Jack and Geiger, James H and MSU)},
abstractNote = {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.},
doi = {10.1021/bi900916t},
url = {https://www.osti.gov/biblio/1006203},
journal = {Biochemistry-US},
issn = {0006-2960},
number = (42) ; 10, 2009,
volume = 48,
place = {United States},
year = {Wed Nov 17 00:00:00 EST 2010},
month = {Wed Nov 17 00:00:00 EST 2010}
}