5IG1

Crystal structure of S. rosetta CaMKII kinase domain

Summary for 5IG1

• Entry DOI: 10.2210/pdb5ig1/pdb
• Related: 5IG0 5IG3 5IG4 5IG5
• Descriptor: CAMK/CAMK2 protein kinase, PHOSPHATE ION (3 entities in total)
• Functional Keywords: ca2+/cam-dependent kinase, choanoflagellate, transferase
• Biological source: Salpingoeca rosetta
• Total number of polymer chains: 2
• Total formula weight: 78585.04

Authors

Bhattacharyya, M.,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

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: 26949248
DOI: 10.7554/eLife.13405

Experimental method

X-RAY DIFFRACTION (2.9 Å)