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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.

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.

SUBMITTER: Kozlov G

PROVIDER: S-EPMC420497 | biostudies-literature | 2004 May

REPOSITORIES: biostudies-literature

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Structure of GlgS from Escherichia coli suggests a role in protein-protein interactions.

Kozlov Guennadi G Elias Demetra D Cygler Miroslaw M Gehring Kalle K

BMC biology 20040525

<h4>Background</h4>The Escherichia coli protein GlgS is up-regulated in response to starvation stress and its overexpression was shown to stimulate glycogen synthesis.<h4>Results</h4>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.<h4>Conclusion</h4>GlgS shows structural homology to Huntingtin, elongation fact ...[more]

PMID: 15161493

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