2f86
From Proteopedia
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The Association Domain of C. elegans CaMKII
Overview
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.
About this Structure
2F86 is a Single protein structure of sequence from Caenorhabditis elegans. Full crystallographic information is available from OCA.
Reference
Oligomerization states of the association domain and the holoenyzme of Ca2+/CaM kinase II., Rosenberg OS, Deindl S, Comolli LR, Hoelz A, Downing KH, Nairn AC, Kuriyan J, FEBS J. 2006 Feb;273(4):682-94. PMID:16441656
Page seeded by OCA on Tue Jan 29 19:29:56 2008
