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

From National Research Council Canada

DOIResolve DOI: https://doi.org/10.1186/1741-7007-2-10
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Name affiliation
  1. National Research Council of Canada. NRC Biotechnology Research Institute
FormatText, Article
SubjectEscherichia coli; pharmaceutical; NMR structure; GlgS; Eschericha coli; glycogen synthesis; protein-protein interactions
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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  • BMC Biology 2 (25 May 2004): 10-1–10-7.
LanguageEnglish
NRC number46208
NPARC number3539805
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