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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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Affiliation
  1. National Research Council of Canada. NRC Biotechnology Research Institute
FormatText, Article
Subjectpharmaceutical; NMR structure; GlgS; glycogen synthesis; protein-protein interactions; Escherichia coli
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.
Publication date
In
  • BMC Biology 2 (25 May 2004): 10-1–10-7.
LanguageEnglish
Peer reviewedYes
NRC numberNRC-BRI-46208
NPARC number3539805
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Record identifierad1275dd-446b-4ee9-9ab4-fd44554a69c1
Record created2009-03-01
Record modified2022-11-18
Date modified: