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

Authors
Journal
BMC Biology
1741-7007
Publisher
Springer (Biomed Central Ltd.)
Publication Date
Volume
2
Issue
1
Identifiers
DOI: 10.1186/1741-7007-2-10
Keywords
  • Research Article
Disciplines
  • Biology

Abstract

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

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