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2f86

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(New page: 200px<br /><applet load="2f86" size="350" color="white" frame="true" align="right" spinBox="true" caption="2f86, resolution 2.64&Aring;" /> '''The Association Doma...)
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==Overview==
==Overview==
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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.
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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==
==About this Structure==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Kuriyan, J.]]
[[Category: Kuriyan, J.]]
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[[Category: Rosenberg, O.S.]]
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[[Category: Rosenberg, O S.]]
[[Category: unc-43; oligomerization domain]]
[[Category: unc-43; oligomerization domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 19:29:56 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:18:43 2008''

Revision as of 15:18, 21 February 2008

Image:2f86.gif

2f86, resolution 2.64Å

Drag the structure with the mouse to rotate

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

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