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| | <StructureSection load='4yua' size='340' side='right'caption='[[4yua]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='4yua' size='340' side='right'caption='[[4yua]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4yua]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YUA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YUA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4yua]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YUA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YUA FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=REF:2,3,7,8-TETRAHYDROXYCHROMENO[5,4,3-CDE]CHROMENE-5,10-DIONE'>REF</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=REF:2,3,7,8-TETRAHYDROXYCHROMENO[5,4,3-CDE]CHROMENE-5,10-DIONE'>REF</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphorylase Phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.1 2.4.1.1] </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=4yua FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yua OCA], [https://pdbe.org/4yua PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yua RCSB], [https://www.ebi.ac.uk/pdbsum/4yua PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yua ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4yua FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yua OCA], [http://pdbe.org/4yua PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4yua RCSB], [http://www.ebi.ac.uk/pdbsum/4yua PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4yua ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PYGM_RABIT PYGM_RABIT]] Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties. | + | [https://www.uniprot.org/uniprot/PYGM_RABIT PYGM_RABIT] Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Oryctolagus cuniculus]] | | [[Category: Oryctolagus cuniculus]] |
| - | [[Category: Phosphorylase]]
| + | [[Category: Chatzileontiadou SMD]] |
| - | [[Category: Chatzileontiadou, S M.D]] | + | [[Category: Kantsadi LA]] |
| - | [[Category: Kantsadi, L A]] | + | [[Category: Kyriakis E]] |
| - | [[Category: Kyriakis, E]] | + | [[Category: Leonidas DD]] |
| - | [[Category: Leonidas, D D]] | + | [[Category: Stravodimos AG]] |
| - | [[Category: Stravodimos, A G]] | + | |
| - | [[Category: Alpha and beta protein]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
PYGM_RABIT Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.
Publication Abstract from PubMed
We present a study on the binding of gallic acid and its dimer ellagic acid to glycogen phosphorylase (GP). Ellagic acid is a potent inhibitor with Kis of 13.4 and 7.5muM, in contrast to gallic acid which displays Kis of 1.7 and 3.9mM for GPb and GPa, respectively. Both compounds are competitive inhibitors with respect to the substrate, glucose-1-phoshate, and non-competitive to the allosteric activator, AMP. However, only ellagic acid functions with glucose in a strongly synergistic mode. The crystal structures of the GPb-gallic acid and GPb-ellagic acid complexes were determined at high resolution, revealing that both ligands bind to the inhibitor binding site of the enzyme and highlight the structural basis for the significant difference in their inhibitory potency.
Natural flavonoids as antidiabetic agents. The binding of gallic and ellagic acids to glycogen phosphorylase b.,Kyriakis E, Stravodimos GA, Kantsadi AL, Chatzileontiadou DS, Skamnaki VT, Leonidas DD FEBS Lett. 2015 May 14. pii: S0014-5793(15)00389-0. doi:, 10.1016/j.febslet.2015.05.013. PMID:25980608[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kyriakis E, Stravodimos GA, Kantsadi AL, Chatzileontiadou DS, Skamnaki VT, Leonidas DD. Natural flavonoids as antidiabetic agents. The binding of gallic and ellagic acids to glycogen phosphorylase b. FEBS Lett. 2015 May 14. pii: S0014-5793(15)00389-0. doi:, 10.1016/j.febslet.2015.05.013. PMID:25980608 doi:http://dx.doi.org/10.1016/j.febslet.2015.05.013
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