5IG4
Crystal structure of N. vectensis CaMKII-A hub
Summary for 5IG4
| Entry DOI | 10.2210/pdb5ig4/pdb |
| Related | 5IG0 5IG1 5IG3 5IG5 |
| Descriptor | Predicted protein, GLYCEROL (3 entities in total) |
| Functional Keywords | ca2+/cam-dependent kinase, sea anemone, closed-ring, transferase |
| Biological source | Nematostella vectensis (Starlet sea anemone) |
| Total number of polymer chains | 7 |
| Total formula weight | 115014.54 |
| Authors | Bhattacharyya, M.,Pappireddi, N.,Gee, C.L.,Barros, T.,Kuriyan, J. (deposition date: 2016-02-26, release date: 2016-03-23, Last modification date: 2023-09-27) |
| Primary citation | Bhattacharyya, M.,Stratton, M.M.,Going, C.C.,McSpadden, E.D.,Huang, Y.,Susa, A.C.,Elleman, A.,Cao, Y.M.,Pappireddi, N.,Burkhardt, P.,Gee, C.L.,Barros, T.,Schulman, H.,Williams, E.R.,Kuriyan, J. Molecular mechanism of activation-triggered subunit exchange in Ca(2+)/calmodulin-dependent protein kinase II. Elife, 5:-, 2016 Cited by PubMed Abstract: 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. PubMed: 26949248DOI: 10.7554/eLife.13405 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.35 Å) |
Structure validation
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