1rrz
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Solution structure of GlgS protein from E. coli
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Structural highlights
FunctionGLGS_ECOLI Involved in glycogen synthesis. May be involved in glycogen priming. Publication Abstract from PubMedBACKGROUND: 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 AlsoReferences
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