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| | <StructureSection load='2phk' size='340' side='right'caption='[[2phk]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='2phk' size='340' side='right'caption='[[2phk]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2phk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/European_rabbit European rabbit]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PHK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PHK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2phk]] is a 2 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=2PHK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PHK FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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]] 2.6Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PHKG ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9986 European rabbit])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phosphorylase_kinase Phosphorylase kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.19 2.7.11.19] </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=2phk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2phk OCA], [https://pdbe.org/2phk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2phk RCSB], [https://www.ebi.ac.uk/pdbsum/2phk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2phk 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=2phk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2phk OCA], [https://pdbe.org/2phk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2phk RCSB], [https://www.ebi.ac.uk/pdbsum/2phk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2phk ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/PHKG1_RABIT PHKG1_RABIT]] Catalytic subunit of the phosphorylase b kinase (PHK), which mediates the neural and hormonal regulation of glycogen breakdown (glycogenolysis) by phosphorylating and thereby activating glycogen phosphorylase. In vitro, phosphorylates PYGM, TNNI3, MAPT/TAU, GAP43 and NRGN/RC3.<ref>PMID:8454596</ref> <ref>PMID:8999860</ref>
| + | [https://www.uniprot.org/uniprot/PHKG1_RABIT PHKG1_RABIT] Catalytic subunit of the phosphorylase b kinase (PHK), which mediates the neural and hormonal regulation of glycogen breakdown (glycogenolysis) by phosphorylating and thereby activating glycogen phosphorylase. In vitro, phosphorylates PYGM, TNNI3, MAPT/TAU, GAP43 and NRGN/RC3.<ref>PMID:8454596</ref> <ref>PMID:8999860</ref> |
| | == 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: European rabbit]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Phosphorylase kinase]] | + | [[Category: Oryctolagus cuniculus]] |
| - | [[Category: Johnson, L N]] | + | [[Category: Johnson LN]] |
| - | [[Category: Lowe, E D]] | + | [[Category: Lowe ED]] |
| - | [[Category: Noble, M E.M]] | + | [[Category: Noble MEM]] |
| - | [[Category: Oikonomakos, N G]] | + | [[Category: Oikonomakos NG]] |
| - | [[Category: Owen, D J]] | + | [[Category: Owen DJ]] |
| - | [[Category: Skamnaki, V T]] | + | [[Category: Skamnaki VT]] |
| - | [[Category: Catalytic mechanism]]
| + | |
| - | [[Category: Dimerization]]
| + | |
| - | [[Category: Reversible phosphorylisation]]
| + | |
| - | [[Category: Substrate recognition]]
| + | |
| Structural highlights
Function
PHKG1_RABIT Catalytic subunit of the phosphorylase b kinase (PHK), which mediates the neural and hormonal regulation of glycogen breakdown (glycogenolysis) by phosphorylating and thereby activating glycogen phosphorylase. In vitro, phosphorylates PYGM, TNNI3, MAPT/TAU, GAP43 and NRGN/RC3.[1] [2]
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
The structure of a truncated form of the gamma-subunit of phosphorylase kinase (PHKgammat) has been solved in a ternary complex with a non-hydrolysable ATP analogue (adenylyl imidodiphosphate, AMPPNP) and a heptapeptide substrate related in sequence to both the natural substrate and to the optimal peptide substrate. Kinetic characterization of the phosphotransfer reaction confirms the peptide to be a good substrate, and the structure allows identification of key features responsible for its high affinity. Unexpectedly, the substrate peptide forms a short anti-parallel beta-sheet with the kinase activation segment, the region which in other kinases plays an important role in regulation of enzyme activity. This anchoring of the main chain of the substrate peptide at a fixed distance from the gamma-phosphate of ATP explains the selectivity of PHK for serine/threonine over tyrosine as a substrate. The catalytic core of PHK exists as a dimer in crystals of the ternary complex, and the relevance of this phenomenon to its in vivo recognition of dimeric glycogen phosphorylase b is considered.
The crystal structure of a phosphorylase kinase peptide substrate complex: kinase substrate recognition.,Lowe ED, Noble ME, Skamnaki VT, Oikonomakos NG, Owen DJ, Johnson LN EMBO J. 1997 Nov 17;16(22):6646-58. PMID:9362479[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Paudel HK, Zwiers H, Wang JH. Phosphorylase kinase phosphorylates the calmodulin-binding regulatory regions of neuronal tissue-specific proteins B-50 (GAP-43) and neurogranin. J Biol Chem. 1993 Mar 25;268(9):6207-13. PMID:8454596
- ↑ Paudel HK. The regulatory Ser262 of microtubule-associated protein tau is phosphorylated by phosphorylase kinase. J Biol Chem. 1997 Jan 17;272(3):1777-85. PMID:8999860
- ↑ Lowe ED, Noble ME, Skamnaki VT, Oikonomakos NG, Owen DJ, Johnson LN. The crystal structure of a phosphorylase kinase peptide substrate complex: kinase substrate recognition. EMBO J. 1997 Nov 17;16(22):6646-58. PMID:9362479 doi:10.1093/emboj/16.22.6646
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