1rrz

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(New page: 200px<br /><applet load="1rrz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rrz" /> '''Solution structure of GlgS protein from E. c...)
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[[Image:1rrz.gif|left|200px]]<br /><applet load="1rrz" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1rrz.gif|left|200px]]<br /><applet load="1rrz" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1rrz" />
caption="1rrz" />
'''Solution structure of GlgS protein from E. coli'''<br />
'''Solution structure of GlgS protein from E. coli'''<br />
==Overview==
==Overview==
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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.
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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.
==About this Structure==
==About this Structure==
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1RRZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RRZ OCA].
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1RRZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RRZ OCA].
==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: BSGI, Montreal-Kingston.Bacterial.Structural.Genomics.Initiative.]]
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[[Category: BSGI, Montreal-Kingston Bacterial Structural Genomics Initiative.]]
[[Category: Gehring, K.]]
[[Category: Gehring, K.]]
[[Category: Kozlov, G.]]
[[Category: Kozlov, G.]]
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[[Category: structural genomics]]
[[Category: structural genomics]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:49:51 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:53:56 2008''

Revision as of 12:53, 21 February 2008


1rrz

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Solution structure of GlgS protein from E. coli

Overview

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.

About this Structure

1RRZ is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structure of GlgS from Escherichia coli suggests a role in protein-protein interactions., Kozlov G, Elias D, Cygler M, Gehring K, BMC Biol. 2004 May 25;2:10. PMID:15161493

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