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| | <StructureSection load='5iko' size='340' side='right'caption='[[5iko]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='5iko' size='340' side='right'caption='[[5iko]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5iko]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IKO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IKO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5iko]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IKO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IKO FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 2.5Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PYGB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=5iko FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5iko OCA], [https://pdbe.org/5iko PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5iko RCSB], [https://www.ebi.ac.uk/pdbsum/5iko PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5iko 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=5iko FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5iko OCA], [http://pdbe.org/5iko PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5iko RCSB], [http://www.ebi.ac.uk/pdbsum/5iko PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5iko ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PYGB_HUMAN PYGB_HUMAN]] 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/PYGB_HUMAN PYGB_HUMAN] 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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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Phosphorylase]] | + | [[Category: Haouz A]] |
| - | [[Category: Haouz, A]] | + | [[Category: Li de la Sierra-Gallay I]] |
| - | [[Category: Mathieu, C]] | + | [[Category: Mathieu C]] |
| - | [[Category: Rodrigues-Lima, F]] | + | [[Category: Rodrigues-Lima F]] |
| - | [[Category: Sierra-Gallay, I Li de la]]
| + | [[Category: Xu X]] |
| - | [[Category: Xu, X]] | + | |
| - | [[Category: Allosteric enzyme]]
| + | |
| - | [[Category: Glycogen disease]]
| + | |
| - | [[Category: Glycogen metabolism]]
| + | |
| - | [[Category: Glycogen phosphorylase]]
| + | |
| - | [[Category: Glycosyltransferase]]
| + | |
| - | [[Category: Gp]]
| + | |
| - | [[Category: Nucleotide-binding]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
PYGB_HUMAN 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
Brain glycogen metabolism plays a critical role in major brain functions such as learning or memory consolidation. However, alteration of glycogen metabolism and glycogen accumulation in the brain contributes to neurodegeneration as observed in Lafora disease. Glycogen phosphorylase (GP), a key enzyme in glycogen metabolism, catalyzes the rate-limiting step of glycogen mobilization. Moreover, the allosteric regulation of the three GP isozymes (muscle, liver, and brain) by metabolites and phosphorylation, in response to hormonal signaling, fine-tunes glycogenolysis to fulfill energetic and metabolic requirements. Whereas the structures of muscle and liver GPs have been known for decades, the structure of brain GP (bGP) has remained elusive despite its critical role in brain glycogen metabolism. Here, we report the crystal structure of human bGP in complex with PEG 400 (2.5 A) and in complex with its allosteric activator AMP (3.4 A). These structures demonstrate that bGP has a closer structural relationship with muscle GP, which is also activated by AMP, contrary to liver GP, which is not. Importantly, despite the structural similarities between human bGP and the two other mammalian isozymes, the bGP structures reveal molecular features unique to the brain isozyme that provide a deeper understanding of the differences in the activation properties of these allosteric enzymes by the allosteric effector AMP. Overall, our study further supports that the distinct structural and regulatory properties of GP isozymes contribute to the different functions of muscle, liver, and brain glycogen.
Insights into Brain Glycogen Metabolism: THE STRUCTURE OF HUMAN BRAIN GLYCOGEN PHOSPHORYLASE.,Mathieu C, de la Sierra-Gallay IL, Duval R, Xu X, Cocaign A, Leger T, Woffendin G, Camadro JM, Etchebest C, Haouz A, Dupret JM, Rodrigues-Lima F J Biol Chem. 2016 Aug 26;291(35):18072-83. doi: 10.1074/jbc.M116.738898. Epub, 2016 Jul 8. PMID:27402852[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Mathieu C, de la Sierra-Gallay IL, Duval R, Xu X, Cocaign A, Leger T, Woffendin G, Camadro JM, Etchebest C, Haouz A, Dupret JM, Rodrigues-Lima F. Insights into Brain Glycogen Metabolism: THE STRUCTURE OF HUMAN BRAIN GLYCOGEN PHOSPHORYLASE. J Biol Chem. 2016 Aug 26;291(35):18072-83. doi: 10.1074/jbc.M116.738898. Epub, 2016 Jul 8. PMID:27402852 doi:http://dx.doi.org/10.1074/jbc.M116.738898
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