Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Hub stability in the calcium calmodulin-dependent protein kinase II.
Journal, issue, pages	Commun Biol, Vol. 7, Issue 1, Page 766, Year 2024
Publish date	Jun 25, 2024
Authors	Chih-Ta Chien / Henry Puhl / Steven S Vogel / Justin E Molloy / Wah Chiu / Shahid Khan /
PubMed Abstract	The calcium calmodulin protein kinase II (CaMKII) is a multi-subunit ring assembly with a central hub formed by the association domains. There is evidence for hub polymorphism between and within ...The calcium calmodulin protein kinase II (CaMKII) is a multi-subunit ring assembly with a central hub formed by the association domains. There is evidence for hub polymorphism between and within CaMKII isoforms, but the link between polymorphism and subunit exchange has not been resolved. Here, we present near-atomic resolution cryogenic electron microscopy (cryo-EM) structures revealing that hubs from the α and β isoforms, either standalone or within an β holoenzyme, coexist as 12 and 14 subunit assemblies. Single-molecule fluorescence microscopy of Venus-tagged holoenzymes detects intermediate assemblies and progressive dimer loss due to intrinsic holoenzyme lability, and holoenzyme disassembly into dimers upon mutagenesis of a conserved inter-domain contact. Molecular dynamics (MD) simulations show the flexibility of 4-subunit precursors, extracted in-silico from the β hub polymorphs, encompassing the curvature of both polymorphs. The MD explains how an open hub structure also obtained from the β holoenzyme sample could be created by dimer loss and analysis of its cryo-EM dataset reveals how the gap could open further. An assembly model, considering dimer concentration dependence and strain differences between polymorphs, proposes a mechanism for intrinsic hub lability to fine-tune the stoichiometry of αβ heterooligomers for their dynamic localization within synapses in neurons.
External links	Commun Biol / PubMed:38918547 / PubMed Central
Methods	EM (single particle)
Resolution	2.6 - 8.4 Å
Structure data	40873 8syg EMDB-40873, PDB-8syg: Cryo-EM structure of tetradecameric hub domain of CaMKII alpha Method: EM (single particle) / Resolution: 2.6 Å 40955 8t15 EMDB-40955, PDB-8t15: Cryo-EM structure of dodecameric hub domain of CaMKII alpha Method: EM (single particle) / Resolution: 2.7 Å 40956 8t17 EMDB-40956, PDB-8t17: Cryo-EM structure of tetradecameric hub domain of CaMKII beta Method: EM (single particle) / Resolution: 2.6 Å 40957 8t18 EMDB-40957, PDB-8t18: Cryo-EM structure of dodecameric hub domain of CaMKII beta Method: EM (single particle) / Resolution: 2.6 Å 41070 8t6k EMDB-41070, PDB-8t6k: Cryo-EM structure of tetradecameric CaMKII beta holoenzyme T287A T306A T307A Method: EM (single particle) / Resolution: 3.0 Å 41077 8t6q EMDB-41077, PDB-8t6q: Cryo-EM structure of dodecameric CaMKII beta holoenzyme T287A T306A T307A Method: EM (single particle) / Resolution: 3.5 Å EMDB-43385: Cryo-EM map of close dodecameric CaMKII beta holoenzyme T287A T306A T307A Method: EM (single particle) / Resolution: 8.4 Å
Source	rattus norvegicus (Norway rat) aequorea victoria (jellyfish)
Keywords	SIGNALING PROTEIN / High-order oligomer / Protein Kinase / Signaling / Memory