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

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DOIResolve DOI: http://doi.org/10.1186/1741-7007-2-10
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TypeArticle
Journal titleBMC Biology
Volume2
Pages10-110-7; # of pages: 7
SubjectEscherichia coli; pha; NMR structure; GlgS; Eschericha coli; glycogen synthesis; protein-protein interactions
AbstractBackground: 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
AffiliationNRC Biotechnology Research Institute; National Research Council Canada
Peer reviewedNo
NRC number46208
NPARC number3539805
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Record identifierad1275dd-446b-4ee9-9ab4-fd44554a69c1
Record created2009-03-01
Record modified2016-05-09
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