5IG4

Crystal structure of N. vectensis CaMKII-A hub

5IG4 の概要

• エントリーDOI: 10.2210/pdb5ig4/pdb
• 関連するPDBエントリー: 5IG0 5IG1 5IG3 5IG5
• 分子名称: Predicted protein, GLYCEROL (3 entities in total)
• 機能のキーワード: ca2+/cam-dependent kinase, sea anemone, closed-ring, transferase
• 由来する生物種: Nematostella vectensis (Starlet sea anemone)
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 115014.54

構造登録者

Bhattacharyya, M.,Pappireddi, N.,Gee, C.L.,Barros, T.,Kuriyan, J. (登録日: 2016-02-26, 公開日: 2016-03-23, 最終更新日: 2023-09-27)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.35 Å)