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 bu...

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Detalles Bibliográficos
Autores principales: Kozlov, Guennadi, Elias, Demetra, Cygler, Miroslaw, Gehring, Kalle
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2004
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC420497/
https://www.ncbi.nlm.nih.gov/pubmed/15161493
http://dx.doi.org/10.1186/1741-7007-2-10
Descripción
Sumario: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 α-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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