3guh

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{{Seed}}
 
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[[Image:3guh.png|left|200px]]
 
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==Crystal Structure of Wild-type E.coli GS in complex with ADP and DGM==
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The line below this paragraph, containing "STRUCTURE_3guh", creates the "Structure Box" on the page.
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<StructureSection load='3guh' size='340' side='right'caption='[[3guh]], [[Resolution|resolution]] 2.79&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3guh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GUH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GUH FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.79&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=250:(2R)-2-HYDROXY-3-[4-(2-HYDROXYETHYL)PIPERAZIN-1-YL]PROPANE-1-SULFONIC+ACID'>250</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ASO:1,5-ANHYDROSORBITOL'>ASO</scene>, <scene name='pdbligand=PE3:3,6,9,12,15,18,21,24,27,30,33,36,39-TRIDECAOXAHENTETRACONTANE-1,41-DIOL'>PE3</scene></td></tr>
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{{STRUCTURE_3guh| PDB=3guh | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3guh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3guh OCA], [https://pdbe.org/3guh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3guh RCSB], [https://www.ebi.ac.uk/pdbsum/3guh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3guh ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GLGA_ECOLI GLGA_ECOLI] Synthesizes alpha-1,4-glucan chains using ADP-glucose.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gu/3guh_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3guh ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===Crystal Structure of Wild-type E.coli GS in complex with ADP and DGM===
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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<ref>PMID:19244233</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_19244233}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 3guh" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 19244233 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_19244233}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Escherichia coli K-12]]
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3GUH is a 1 chain 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=3GUH OCA].
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[[Category: Large Structures]]
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[[Category: Geiger J]]
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==Reference==
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[[Category: Sheng F]]
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<ref group="xtra">PMID:19244233</ref><references group="xtra"/>
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[[Category: Escherichia coli]]
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[[Category: Starch synthase]]
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[[Category: Geiger, J.]]
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[[Category: Sheng, F.]]
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[[Category: Adp and intermediate d-glucopyranosylium binding]]
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[[Category: Closed-form]]
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[[Category: Glycogen biosynthesis]]
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[[Category: Glycosyl-transferase]]
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[[Category: Glycosyltransferase]]
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[[Category: Gt-b fold]]
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[[Category: Rossmann fold]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 6 10:40:02 2009''
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Current revision

Crystal Structure of Wild-type E.coli GS in complex with ADP and DGM

PDB ID 3guh

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