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TitleThe CaMKII holoenzyme structure in activation-competent conformations.
Journal, issue, pagesNat Commun, Vol. 8, Page 15742, Year 2017
Publish dateJun 7, 2017
AuthorsJanette B Myers / Vincent Zaegel / Steven J Coultrap / Adam P Miller / K Ulrich Bayer / Steve L Reichow /
PubMed AbstractThe Ca/calmodulin-dependent protein kinase II (CaMKII) assembles into large 12-meric holoenzymes, which is thought to enable regulatory processes required for synaptic plasticity underlying learning, ...The Ca/calmodulin-dependent protein kinase II (CaMKII) assembles into large 12-meric holoenzymes, which is thought to enable regulatory processes required for synaptic plasticity underlying learning, memory and cognition. Here we used single particle electron microscopy (EM) to determine a pseudoatomic model of the CaMKIIα holoenzyme in an extended and activation-competent conformation. The holoenzyme is organized by a rigid central hub complex, while positioning of the kinase domains is highly flexible, revealing dynamic holoenzymes ranging from 15-35 nm in diameter. While most kinase domains are ordered independently, ∼20% appear to form dimers and <3% are consistent with a compact conformation. An additional level of plasticity is revealed by a small fraction of bona-fide 14-mers (<4%) that may enable subunit exchange. Biochemical and cellular FRET studies confirm that the extended state of CaMKIIα resolved by EM is the predominant form of the holoenzyme, even under molecular crowding conditions.
External linksNat Commun / PubMed:28589927 / PubMed Central
MethodsEM (single particle)
Resolution20.0 Å
Structure data

8514

5u6y

EMDB-8514: 3D reconstruction of the CaMKIIa holoenzyme.
PDB-5u6y: Pseudo-atomic model of the CaMKIIa holoenzyme.
Method: EM (single particle) / Resolution: 20.0 Å

Source
  • rattus norvegicus (Norway rat)
KeywordsTRANSFERASE / Calcium/calmodulin-dependent kinase II (CaMKII) / cell signaling / calcium / calmodulin (CaM) / long-term potentiation (LTP) / long-term depression (LTD) / synaptic plasticity / cooperativity / electron microscopy (EM) / single particle reconstruction / intrinsic disorder

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