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Open Access Open Badges Research article

Structure of GlgS from Escherichia coli suggests a role in protein–protein interactions

Guennadi Kozlov1, Demetra Elias1, Miroslaw Cygler2 and Kalle Gehring1*

Author Affiliations

1 Department of Biochemistry, McGill University, Montreal, Quebec H3G 1Y6, Canada

2 Macromolecular Structure Group, Biotechnology Research Institute, National Research Council of Canada, Montreal, Quebec H4P 2R2, Canada

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BMC Biology 2004, 2:10  doi:10.1186/1741-7007-2-10

Published: 25 May 2004



The Escherichia coli protein GlgS is up-regulated in response to starvation stress and its overexpression was shown to stimulate glycogen synthesis.


We solved the structure of GlgS from E. coli, a member of an enterobacterial protein family. The protein structure represents a bundle of three α-helices with a short hydrophobic helix sandwiched between two long amphipathic helices.


GlgS shows structural homology to Huntingtin, elongation factor 3, protein phosphatase 2A, TOR1 motif domains and tetratricopeptide repeats, suggesting a possible role in protein–protein interactions.

NMR structure; GlgS; Escherichia coli; glycogen synthesis; protein–protein interactions.