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
AuthorSearch for: ; Search for: ; Search for: 1; Search for:
Name affiliation
  1. National Research Council of Canada. NRC Biotechnology Research Institute
FormatText, Article
Journal titleBMC Biology
Volume2
Pages10-1–10-7
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.
Publication date
LanguageEnglish
NRC number46208
NPARC number3539805
Export citationExport as RIS
Report a correctionReport a correction
Record identifierad1275dd-446b-4ee9-9ab4-fd44554a69c1
Record created2009-03-01
Record modified2020-04-17
Report a problem on this page
Date modified: