1rrz

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|ACTIVITY=
|ACTIVITY=
|GENE= GLGS, B3049 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
|GENE= GLGS, B3049 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rrz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rrz OCA], [http://www.ebi.ac.uk/pdbsum/1rrz PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1rrz RCSB]</span>
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[[Category: structural genomic]]
[[Category: structural genomic]]
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Revision as of 20:32, 30 March 2008


PDB ID 1rrz

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Gene: GLGS, B3049 (Escherichia coli)
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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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