5U6Y
Pseudo-atomic model of the CaMKIIa holoenzyme.
Summary for 5U6Y
| Entry DOI | 10.2210/pdb5u6y/pdb |
| EMDB information | 8514 |
| Descriptor | Calcium/calmodulin-dependent protein kinase type II subunit alpha (1 entity in total) |
| Functional Keywords | calcium/calmodulin-dependent kinase ii (camkii), cell signaling, calcium, calmodulin (cam), long-term potentiation (ltp), long-term depression (ltd), synaptic plasticity, cooperativity, electron microscopy (em), single particle reconstruction, intrinsic disorder, transferase |
| Biological source | Rattus norvegicus (Rat) |
| Total number of polymer chains | 12 |
| Total formula weight | 627378.42 |
| Authors | Myers, J.,Reichow, S.L. (deposition date: 2016-12-09, release date: 2017-06-21, Last modification date: 2024-03-13) |
| Primary citation | Myers, J.B.,Zaegel, V.,Coultrap, S.J.,Miller, A.P.,Bayer, K.U.,Reichow, S.L. The CaMKII holoenzyme structure in activation-competent conformations. Nat Commun, 8:15742-15742, 2017 Cited by PubMed Abstract: The Ca/calmodulin-dependent protein kinase II (CaMKII) assembles into large 12-meric holoenzymes, which is thought to enable regulatory processes required for synaptic plasticity underlying learning, memory and cognition. Here we used single particle electron microscopy (EM) to determine a pseudoatomic model of the CaMKIIα holoenzyme in an extended and activation-competent conformation. The holoenzyme is organized by a rigid central hub complex, while positioning of the kinase domains is highly flexible, revealing dynamic holoenzymes ranging from 15-35 nm in diameter. While most kinase domains are ordered independently, ∼20% appear to form dimers and <3% are consistent with a compact conformation. An additional level of plasticity is revealed by a small fraction of bona-fide 14-mers (<4%) that may enable subunit exchange. Biochemical and cellular FRET studies confirm that the extended state of CaMKIIα resolved by EM is the predominant form of the holoenzyme, even under molecular crowding conditions. PubMed: 28589927DOI: 10.1038/ncomms15742 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (20 Å) |
Structure validation
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