Structure of GlgS from Escherichia coli suggests a role in protein-protein interactions.
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.
Kozlov
Guennadi
G
Department of Biochemistry, McGill University, Montreal, Quebec H3G 1Y6, Canada. guennadi.kozlov@mcgill.ca
Elias
Demetra
D
Cygler
Miroslaw
M
Gehring
Kalle
K
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
D029968:Escherichia coli Proteins; C098049:GlgS protein, E coli; D006003:Glycogen