5IG5

Crystal structure of N. vectensis CaMKII-B hub at pH 4.2

Summary for 5IG5

• Entry DOI: 10.2210/pdb5ig5/pdb
• Related: 5IG0 5IG1 5IG3 5IG4
• Descriptor: CaMKII-B hub (2 entities in total)
• Functional Keywords: ca2+/cam-dependent kinase, sea anemone, peptide docking, open-spiral, transferase
• Biological source: Nematostella vectensis (Starlet sea anemone)
• Total number of polymer chains: 7
• Total formula weight: 115805.03

Authors

Bhattacharyya, M.,Gee, C.L.,Barros, T.,Kuriyan, J. (deposition date: 2016-02-26, release date: 2016-03-23, Last modification date: 2024-10-23)

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 (3 Å)