1rrz
From Proteopedia
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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" /> | ||
| - | '''Solution structure of GlgS protein from E. coli'''<br /> | ||
| - | == | + | ==Solution structure of GlgS protein from E. coli== |
| + | <StructureSection load='1rrz' size='340' side='right'caption='[[1rrz]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1rrz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RRZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RRZ FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1rrz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rrz OCA], [https://pdbe.org/1rrz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rrz RCSB], [https://www.ebi.ac.uk/pdbsum/1rrz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rrz ProSAT], [https://www.topsan.org/Proteins/BSGI/1rrz TOPSAN]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/GLGS_ECOLI GLGS_ECOLI] Involved in glycogen synthesis. May be involved in glycogen priming. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
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. | 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. | ||
| - | + | 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<ref>PMID:15161493</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1rrz" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Green Fluorescent Protein 3D structures|Green Fluorescent Protein 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Gehring K]] | ||
| + | [[Category: Kozlov G]] | ||
Current revision
Solution structure of GlgS protein from E. coli
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