2F86

The Association Domain of C. elegans CaMKII

Summary for 2F86

• Entry DOI: 10.2210/pdb2f86/pdb
• Descriptor: Hypothetical protein K11E8.1d (2 entities in total)
• Functional Keywords: unc-43; oligomerization domain, transferase
• Biological source: Caenorhabditis elegans
• Cellular location: Cytoplasm : O62305
• Total number of polymer chains: 7
• Total formula weight: 115236.28

Authors

Rosenberg, O.S.,Kuriyan, J. (deposition date: 2005-12-01, release date: 2006-02-07, Last modification date: 2023-08-30)

Primary citation

Rosenberg, O.S.,Deindl, S.,Comolli, L.R.,Hoelz, A.,Downing, K.H.,Nairn, A.C.,Kuriyan, J.
Oligomerization states of the association domain and the holoenyzme of Ca2+/CaM kinase II.
Febs J., 273:682-694, 2006

PubMed Abstract: Ca2+/calmodulin activated protein kinase II (CaMKII) is an oligomeric protein kinase with a unique holoenyzme architecture. The subunits of CaMKII are bound together into the holoenzyme by the association domain, a C-terminal region of approximately 140 residues in the CaMKII polypeptide. Single particle analyses of electron micrographs have suggested previously that the holoenyzme forms a dodecamer that contains two stacked 6-fold symmetric rings. In contrast, a recent crystal structure of the isolated association domain of mouse CaMKIIalpha has revealed a tetradecameric assembly with two stacked 7-fold symmetric rings. In this study, we have determined the crystal structure of the Caenorhabditis elegans CaMKII association domain and it too forms a tetradecamer. We also show by electron microscopy that in its fully assembled form the CaMKII holoenzyme is a dodecamer but without the kinase domains, either from expression of the isolated association domain in bacteria or following their removal by proteolysis, the association domains form a tetradecamer. We speculate that the holoenzyme is held in its 6-fold symmetric state by the interactions of the N-terminal approximately 1-335 residues and that the removal of this region allows the association domain to convert into a more stable 7-fold symmetric form.

PubMed: 16441656
DOI: 10.1111/j.1742-4658.2005.05088.x

Experimental method

X-RAY DIFFRACTION (2.64 Å)