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| | <StructureSection load='5w5t' size='340' side='right'caption='[[5w5t]], [[Resolution|resolution]] 1.76Å' scene=''> | | <StructureSection load='5w5t' size='340' side='right'caption='[[5w5t]], [[Resolution|resolution]] 1.76Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5w5t]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/"achromobacter_radiobacter"_(beijerinck_and_van_delden_1902)_bergey_et_al._1934 "achromobacter radiobacter" (beijerinck and van delden 1902) bergey et al. 1934]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5W5T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5W5T FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5w5t]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Agrobacterium_tumefaciens Agrobacterium tumefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5W5T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5W5T FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9X7:ethyl+2-oxopropanoate'>9X7</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 1.76Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[5w6j|5w6j]], [[5w5r|5w5r]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9X7:ethyl+2-oxopropanoate'>9X7</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">glgC ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=358 "Achromobacter radiobacter" (Beijerinck and van Delden 1902) Bergey et al. 1934])</td></tr> | + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glucose-1-phosphate_adenylyltransferase Glucose-1-phosphate adenylyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.27 2.7.7.27] </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=5w5t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5w5t OCA], [https://pdbe.org/5w5t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5w5t RCSB], [https://www.ebi.ac.uk/pdbsum/5w5t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5w5t 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=5w5t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5w5t OCA], [https://pdbe.org/5w5t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5w5t RCSB], [https://www.ebi.ac.uk/pdbsum/5w5t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5w5t ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/GLGC_RHIRD GLGC_RHIRD]] Catalyzes the synthesis of ADP-glucose, a sugar donor used in elongation reactions on alpha-glucans.
| + | [https://www.uniprot.org/uniprot/GLGC_RHIRD GLGC_RHIRD] Catalyzes the synthesis of ADP-glucose, a sugar donor used in elongation reactions on alpha-glucans. |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | The pathways for biosynthesis of glycogen in bacteria and starch in plants are evolutionarily and biochemically related. They are regulated primarily by ADP-glucose pyrophosphorylase, which evolved to satisfy metabolic requirements of a particular organism. Despite the importance of these two pathways, little is known about the mechanism that controls pyrophosphorylase activity or the location of its allosteric sites. Here, we report pyruvate-bound crystal structures of ADP-glucose pyrophosphorylase from the bacterium Agrobacterium tumefaciens, identifying a previously elusive activator site for the enzyme. We found that the tetrameric enzyme binds two molecules of pyruvate in a planar conformation. Each binding site is located in a crevice between the C-terminal domains of two subunits where they stack via a distinct beta-helix region. Pyruvate interacts with the side chain of Lys-43 and with the peptide backbone of Ser-328 and Gly-329 from both subunits. These structural insights led to the design of two variants with altered regulatory properties. In one variant (K43A), the allosteric effect was absent, whereas in the other (G329D), the introduced Asp mimicked the presence of pyruvate. The latter generated an enzyme that was pre-activated and insensitive to further activation by pyruvate. Our study furnishes a deeper understanding of how glycogen biosynthesis is regulated in bacteria and the mechanism by which transgenic plants increased their starch production. These insights will facilitate rational approaches to enzyme engineering for starch production in crops of agricultural interest and will promote further study of allosteric signal transmission and molecular evolution in this important enzyme family.
| + | |
| - | | + | |
| - | Structural analysis reveals a pyruvate-binding activator site in the Agrobacterium tumefaciens ADP-glucose pyrophosphorylase.,Hill BL, Mascarenhas R, Patel HP, Asencion Diez MD, Wu R, Iglesias AA, Liu D, Ballicora MA J Biol Chem. 2018 Nov 6. pii: RA118.004246. doi: 10.1074/jbc.RA118.004246. PMID:30401744<ref>PMID:30401744</ref>
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| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 5w5t" style="background-color:#fffaf0;"></div>
| + | |
| - | == References ==
| + | |
| - | <references/>
| + | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Glucose-1-phosphate adenylyltransferase]] | + | [[Category: Agrobacterium tumefaciens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ballicora, M A]] | + | [[Category: Ballicora MA]] |
| - | [[Category: Hill, B L]] | + | [[Category: Hill BL]] |
| - | [[Category: Liu, D]] | + | [[Category: Liu D]] |
| - | [[Category: Mascarenhas, R N]] | + | [[Category: Mascarenhas RN]] |
| - | [[Category: Allosterism]]
| + | |
| - | [[Category: Glycogen biosynthesis]]
| + | |
| - | [[Category: Starch biosynthesis]]
| + | |
| - | [[Category: Transferase]]
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