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
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author Kozlov, Guennadi
Elias, Demetra
Cygler, Miroslaw
Gehring, Kalle
author_facet Kozlov, Guennadi
Elias, Demetra
Cygler, Miroslaw
Gehring, Kalle
author_sort Kozlov, Guennadi
collection PubMed
description 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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spelling pubmed-4204972004-06-11 Structure of GlgS from Escherichia coli suggests a role in protein–protein interactions Kozlov, Guennadi Elias, Demetra Cygler, Miroslaw Gehring, Kalle BMC Biol Research Article 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. BioMed Central 2004-05-25 /pmc/articles/PMC420497/ /pubmed/15161493 http://dx.doi.org/10.1186/1741-7007-2-10 Text en Copyright © 2004 Kozlov et al; licensee BioMed Central Ltd. This is an Open Access article: verbatim copying and redistribution of this article are permitted in all media for any purpose, provided this notice is preserved along with the article's original URL.
spellingShingle Research Article
Kozlov, Guennadi
Elias, Demetra
Cygler, Miroslaw
Gehring, Kalle
Structure of GlgS from Escherichia coli suggests a role in protein–protein interactions
title Structure of GlgS from Escherichia coli suggests a role in protein–protein interactions
title_full Structure of GlgS from Escherichia coli suggests a role in protein–protein interactions
title_fullStr Structure of GlgS from Escherichia coli suggests a role in protein–protein interactions
title_full_unstemmed Structure of GlgS from Escherichia coli suggests a role in protein–protein interactions
title_short Structure of GlgS from Escherichia coli suggests a role in protein–protein interactions
title_sort structure of glgs from escherichia coli suggests a role in protein–protein interactions
topic Research Article
url 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
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