Structure of GlgS from Escherichia coli suggests a role in protein-protein interactions
Guennadi Kozlov1, Demetra Elias, Miroslaw Cygler
1Department of Biochemistry, McGill University, Montreal, Quebec H3G 1Y6, Canada. guennadi.kozlov@mcgill.ca
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 alpha-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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