title: Structure of GlgS from Escherichia coli suggests a role in protein-protein interactions.
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 alpha-helices with a short hydrophobic helix sandwiched between two long amphipathic helices.
  
  
  CONCLUSIONS
  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.
authors.affiliation: Department of Biochemistry, McGill University, Montreal, Quebec H3G 1Y6, Canada. guennadi.kozlov@mcgill.ca
authors.forename: Guennadi
authors.initials: G
authors.lastname: Kozlov
authors.forename: Demetra
authors.initials: D
authors.lastname: Elias
authors.forename: Miroslaw
authors.initials: M
authors.lastname: Cygler
authors.forename: Kalle
authors.initials: K
authors.lastname: Gehring
mesh_terms: D000595:Amino Acid Sequence; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry*; D006003:Glycogen / Q000096:biosynthesis; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D025941:Protein Interaction Mapping; D017386:Sequence Homology, Amino Acid
chemical_list: D029968:Escherichia coli Proteins; C098049:GlgS protein, E coli; D006003:Glycogen