5ig0: Difference between revisions
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==Crystal structure of S. rosetta CaMKII hub== | ==Crystal structure of S. rosetta CaMKII hub== | ||
<StructureSection load='5ig0' size='340' side='right' caption='[[5ig0]], [[Resolution|resolution]] 1.75Å' scene=''> | <StructureSection load='5ig0' size='340' side='right'caption='[[5ig0]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5ig0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Proterospongia_sp._atcc_50818 Proterospongia sp. atcc 50818]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IG0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IG0 FirstGlance]. <br> | <table><tr><td colspan='2'>[[5ig0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Proterospongia_sp._atcc_50818 Proterospongia sp. atcc 50818]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IG0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IG0 FirstGlance]. <br> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Proterospongia sp. atcc 50818]] | [[Category: Proterospongia sp. atcc 50818]] | ||
[[Category: Barros, T]] | [[Category: Barros, T]] | ||
Revision as of 19:17, 20 November 2019
Crystal structure of S. rosetta CaMKII hubCrystal structure of S. rosetta CaMKII hub
Structural highlights
Publication Abstract from PubMedActivation 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. Molecular mechanism of activation-triggered subunit exchange in Ca(2+)/calmodulin-dependent protein kinase II.,Bhattacharyya M, Stratton MM, Going CC, McSpadden ED, Huang Y, Susa AC, Elleman A, Cao YM, Pappireddi N, Burkhardt P, Gee CL, Barros T, Schulman H, Williams ER, Kuriyan J Elife. 2016 Mar 7;5. pii: e13405. doi: 10.7554/eLife.13405. PMID:26949248[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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