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

DOI	Resolve DOI: https://doi.org/10.1186/1741-7007-2-10
Author	Search for: Kozlov, Guennadi; Search for: Elias, Demetra; Search for: Cygler, Miroslaw¹; Search for: Gehring, Kalle
Name affiliation	National Research Council of Canada. NRC Biotechnology Research Institute
Format	Text, Article
Subject	pharmaceutical; 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	2004-05-25
In	BMC Biology 2 (25 May 2004): 10-1–10-7.
Language	English
Peer reviewed	Yes
NRC number	NRC-BRI-46208
NPARC number	3539805
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Record identifier	ad1275dd-446b-4ee9-9ab4-fd44554a69c1
Record created	2009-03-01
Record modified	2022-11-18