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| | <StructureSection load='5ig1' size='340' side='right'caption='[[5ig1]], [[Resolution|resolution]] 2.90Å' scene=''> | | <StructureSection load='5ig1' size='340' side='right'caption='[[5ig1]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ig1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Proterospongia_sp._atcc_50818 Proterospongia sp. atcc 50818]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IG1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IG1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ig1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Salpingoeca_rosetta Salpingoeca rosetta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IG1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IG1 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 2.9Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ig0|5ig0]], [[5ig3|5ig3]], [[5ig4|5ig4]], [[5ig5|5ig5]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PTSG_10090 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=946362 Proterospongia sp. ATCC 50818])</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=5ig1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ig1 OCA], [https://pdbe.org/5ig1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ig1 RCSB], [https://www.ebi.ac.uk/pdbsum/5ig1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ig1 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=5ig1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ig1 OCA], [http://pdbe.org/5ig1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ig1 RCSB], [http://www.ebi.ac.uk/pdbsum/5ig1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ig1 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/F2UPG5_SALR5 F2UPG5_SALR5] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5ig1" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5ig1" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Calcium/calmodulin dependent protein kinase 3D structures|Calcium/calmodulin dependent protein kinase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Proterospongia sp. atcc 50818]] | + | [[Category: Salpingoeca rosetta]] |
| - | [[Category: Barros, T]] | + | [[Category: Barros T]] |
| - | [[Category: Bhattacharyya, M]] | + | [[Category: Bhattacharyya M]] |
| - | [[Category: Gee, C L]] | + | [[Category: Gee CL]] |
| - | [[Category: Kuriyan, J]] | + | [[Category: Kuriyan J]] |
| - | [[Category: Ca2+/cam-dependent kinase]]
| + | |
| - | [[Category: Choanoflagellate]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
F2UPG5_SALR5
Publication Abstract from PubMed
Activation triggers the exchange of subunits in Ca(2+)/calmodulin-dependent protein kinase II (CaMKII), an oligomeric enzyme that is critical for learning, memory, and cardiac function. The mechanism by which subunit exchange occurs remains elusive. We show that the human CaMKII holoenzyme exists in dodecameric and tetradecameric forms, and that the calmodulin (CaM)-binding element of CaMKII can bind to the hub of the holoenzyme and destabilize it to release dimers. The structures of CaMKII from two distantly diverged organisms suggest that the CaM-binding element of activated CaMKII acts as a wedge by docking at intersubunit interfaces in the hub. This converts the hub into a spiral form that can release or gain CaMKII dimers. Our data reveal a three-way competition for the CaM-binding element, whereby phosphorylation biases it towards the hub interface, away from the kinase domain and calmodulin, thus unlocking the ability of activated CaMKII holoenzymes to exchange dimers with unactivated ones.
Molecular mechanism of activation-triggered subunit exchange in Ca(2+)/calmodulin-dependent protein kinase II.,Bhattacharyya M, Stratton MM, Going CC, McSpadden ED, Huang Y, Susa AC, Elleman A, Cao YM, Pappireddi N, Burkhardt P, Gee CL, Barros T, Schulman H, Williams ER, Kuriyan J Elife. 2016 Mar 7;5. pii: e13405. doi: 10.7554/eLife.13405. PMID:26949248[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bhattacharyya M, Stratton MM, Going CC, McSpadden ED, Huang Y, Susa AC, Elleman A, Cao YM, Pappireddi N, Burkhardt P, Gee CL, Barros T, Schulman H, Williams ER, Kuriyan J. Molecular mechanism of activation-triggered subunit exchange in Ca(2+)/calmodulin-dependent protein kinase II. Elife. 2016 Mar 7;5. pii: e13405. doi: 10.7554/eLife.13405. PMID:26949248 doi:http://dx.doi.org/10.7554/eLife.13405
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