Structural highlights
Function
GLGS_ECOLI Involved in glycogen synthesis. May be involved in glycogen priming.
Publication Abstract from PubMed
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.
Structure of GlgS from Escherichia coli suggests a role in protein-protein interactions.,Kozlov G, Elias D, Cygler M, Gehring K BMC Biol. 2004 May 25;2:10. PMID:15161493[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kozlov G, Elias D, Cygler M, Gehring K. Structure of GlgS from Escherichia coli suggests a role in protein-protein interactions. BMC Biol. 2004 May 25;2:10. PMID:15161493 doi:10.1186/1741-7007-2-10