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| | <StructureSection load='3d1j' size='340' side='right'caption='[[3d1j]], [[Resolution|resolution]] 3.00Å' scene=''> | | <StructureSection load='3d1j' size='340' side='right'caption='[[3d1j]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3d1j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D1J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3D1J FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3d1j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D1J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3D1J FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2qyy|2qyy]], [[2qzs|2qzs]], [[2r4u|2r4u]], [[2r4t|2r4t]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">glgA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Starch_synthase Starch synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.21 2.4.1.21] </span></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=3d1j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d1j OCA], [https://pdbe.org/3d1j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3d1j RCSB], [https://www.ebi.ac.uk/pdbsum/3d1j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3d1j ProSAT]</span></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=3d1j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d1j OCA], [https://pdbe.org/3d1j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3d1j RCSB], [https://www.ebi.ac.uk/pdbsum/3d1j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3d1j ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/GLGA_ECOLI GLGA_ECOLI]] Synthesizes alpha-1,4-glucan chains using ADP-glucose.
| + | [https://www.uniprot.org/uniprot/GLGA_ECOLI GLGA_ECOLI] Synthesizes alpha-1,4-glucan chains using ADP-glucose. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Starch synthase]]
| + | [[Category: Geiger JH]] |
| - | [[Category: Geiger, J H]] | + | [[Category: Sheng F]] |
| - | [[Category: Sheng, F]] | + | |
| - | [[Category: Glycogen biosynthesis]]
| + | |
| - | [[Category: Glycosyl-transferase]]
| + | |
| - | [[Category: Glycosyltransferase]]
| + | |
| - | [[Category: Gt-b fold]]
| + | |
| - | [[Category: Open form]]
| + | |
| - | [[Category: Rossmann fold]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
GLGA_ECOLI Synthesizes alpha-1,4-glucan chains using ADP-glucose.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Escherichia coli glycogen synthase (EcGS, EC 2.4.1.21) is a retaining glycosyltransferase (GT) that transfers glucose from adenosine diphosphate glucose to a glucan chain acceptor with retention of configuration at the anomeric carbon. EcGS belongs to the GT-B structural superfamily. Here we report several EcGS x-ray structures that together shed considerable light on the structure and function of these enzymes. The structure of the wild-type enzyme bound to ADP and glucose revealed a 15.2 degrees overall domain-domain closure and provided for the first time the structure of the catalytically active, closed conformation of a glycogen synthase. The main chain carbonyl group of His-161, Arg-300, and Lys-305 are suggested by the structure to act as critical catalytic residues in the transglycosylation. Glu-377, previously thought to be catalytic is found on the alpha-face of the glucose and plays an electrostatic role in the active site and as a glucose ring locator. This is also consistent with the structure of the EcGS(E377A)-ADP-HEPPSO complex where the glucose moiety is either absent or disordered in the active site.
The crystal structures of the open and catalytically competent closed conformation of Escherichia coli glycogen synthase.,Sheng F, Jia X, Yep A, Preiss J, Geiger JH J Biol Chem. 2009 Jun 26;284(26):17796-807. Epub 2009 Feb 25. PMID:19244233[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sheng F, Jia X, Yep A, Preiss J, Geiger JH. The crystal structures of the open and catalytically competent closed conformation of Escherichia coli glycogen synthase. J Biol Chem. 2009 Jun 26;284(26):17796-807. Epub 2009 Feb 25. PMID:19244233 doi:10.1074/jbc.M809804200
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