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- EMDB-41077: Cryo-EM structure of dodecameric CaMKII beta holoenzyme T287A T30... -
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Open data
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Basic information
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Title | Cryo-EM structure of dodecameric CaMKII beta holoenzyme T287A T306A T307A | |||||||||
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![]() | High-order oligomer / Protein Kinase / Signaling / Memory / SIGNALING PROTEIN | |||||||||
Function / homology | ![]() regulation of synaptic transmission, cholinergic / activation of meiosis involved in egg activation / cell projection morphogenesis / HSF1-dependent transactivation / RAF activation / Ion transport by P-type ATPases / hippocampal neuron apoptotic process / calcium- and calmodulin-dependent protein kinase complex / cellular response to homocysteine / Interferon gamma signaling ...regulation of synaptic transmission, cholinergic / activation of meiosis involved in egg activation / cell projection morphogenesis / HSF1-dependent transactivation / RAF activation / Ion transport by P-type ATPases / hippocampal neuron apoptotic process / calcium- and calmodulin-dependent protein kinase complex / cellular response to homocysteine / Interferon gamma signaling / positive regulation of synapse maturation / regulation of neuron migration / Ca2+/calmodulin-dependent protein kinase / structural constituent of postsynaptic actin cytoskeleton / regulation of synapse maturation / positive regulation of dendritic spine morphogenesis / calcium-dependent protein serine/threonine kinase activity / Trafficking of AMPA receptors / RAF/MAP kinase cascade / calmodulin-dependent protein kinase activity / response to psychosocial stress / Ion homeostasis / phospholipase binding / neuromuscular process controlling balance / Unblocking of NMDA receptors, glutamate binding and activation / regulation of protein localization to plasma membrane / spindle midzone / response to cadmium ion / sarcoplasmic reticulum membrane / bioluminescence / generation of precursor metabolites and energy / long-term synaptic potentiation / positive regulation of apoptotic signaling pathway / apoptotic signaling pathway / regulation of long-term neuronal synaptic plasticity / positive regulation of neuron projection development / G1/S transition of mitotic cell cycle / calcium ion transport / nervous system development / perikaryon / peptidyl-serine phosphorylation / protein autophosphorylation / postsynaptic density / cell differentiation / calmodulin binding / neuron projection / protein serine kinase activity / protein serine/threonine kinase activity / centrosome / glutamatergic synapse / dendrite / protein kinase binding / protein homodimerization activity / ATP binding / identical protein binding / cytoplasm / cytosol Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.5 Å | |||||||||
![]() | Chien C-T / Chiu W / Khan S | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Hub stability in the calcium calmodulin dependent protein kinase II Authors: Chien C-T / Puhl H / Vogel SS / Molloy J / Chiu W / Khan S | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 117.8 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 13.8 KB 13.8 KB | Display Display | ![]() |
Images | ![]() | 55 KB | ||
Filedesc metadata | ![]() | 5.7 KB | ||
Others | ![]() ![]() | 116 MB 116 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 918.7 KB | Display | ![]() |
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Full document | ![]() | 918.3 KB | Display | |
Data in XML | ![]() | 13.8 KB | Display | |
Data in CIF | ![]() | 16.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8t6qMC ![]() 8sygC ![]() 8t15C ![]() 8t17C ![]() 8t18C ![]() 8t6kC C: citing same article ( M: atomic model generated by this map |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.86 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_41077_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_41077_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Venus-tagged CaMKII beta holoenzyme T287A T306A T307A
Entire | Name: Venus-tagged CaMKII beta holoenzyme T287A T306A T307A |
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Components |
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-Supramolecule #1: Venus-tagged CaMKII beta holoenzyme T287A T306A T307A
Supramolecule | Name: Venus-tagged CaMKII beta holoenzyme T287A T306A T307A / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: Venus-tagged CaMKII beta holoenzyme mutant
Macromolecule | Name: Venus-tagged CaMKII beta holoenzyme mutant / type: protein_or_peptide / ID: 1 / Number of copies: 12 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 90.846859 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MGSSHHHHHH SSGLVPRGSH VSKGEELFTG VVPILVELDG DVNGHKFSVS GEGEGDATYG KLTLKLICTT GKLPVPWPTL VTTLGYGLQ CFARYPDHMK QHDFFKSAMP EGYVQERTIF FKDDGNYKTR AEVKFEGDTL VNRIELKGID FKEDGNILGH K LEYNYNSH ...String: MGSSHHHHHH SSGLVPRGSH VSKGEELFTG VVPILVELDG DVNGHKFSVS GEGEGDATYG KLTLKLICTT GKLPVPWPTL VTTLGYGLQ CFARYPDHMK QHDFFKSAMP EGYVQERTIF FKDDGNYKTR AEVKFEGDTL VNRIELKGID FKEDGNILGH K LEYNYNSH NVYITADKQK NGIKANFKIR HNIEDGGVQL ADHYQQNTPI GDGPVLLPDN HYLSYQSKLS KDPNEKRDHM VL LEFVTAA GITLGMDELY KSGLRSRAQA SNSAVDMATT VTCTRFTDEY QLYEDIGKGA FSVVRRCVKL CTGHEYAAKI INT KKLSAR DHQKLEREAR ICRLLKHSNI VRLHDSISEE GFHYLVFDLV TGGELFEDIV AREYYSEADA SHCIQQILEA VLHC HQMGV VHRDLKPENL LLASKCKGAA VKLADFGLAI EVQGDQQAWF GFAGTPGYLS PEVLRKEAYG KPVDIWACGV ILYIL LVGY PPFWDEDQHK LYQQIKAGAY DFPSPEWDTV TPEAKNLINQ MLTINPAKRI TAHEALKHPW VCQRSTVASM MHRQEA VEC LKKFNARRKL KGAILAAMLA TRNFSVGRQT TAPATMSTAA SGTTMGLVEQ AKSLLNKKAD GVKPQTNSTK NSSAITS PK GSLPPAALEP QTTVIHNPVD GIKESSDSTN TTIEDEDAKA RKQEIIKTTE QLIEAVNNGD FEAYAKICDP GLTSFEPE A LGNLVEGMDF HRFYFENLLA KNSKPIHTTI LNPHVHVIGE DAACIAYIRL TQYIDGQGRP RTSQSEETRV WHRPDGKWQ NVHFHCSGAP VAPLQ UniProtKB: Green fluorescent protein, Calcium/calmodulin-dependent protein kinase type II subunit beta |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Concentration | 20 mg/mL |
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Buffer | pH: 7.5 |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 60.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.5 µm / Nominal defocus min: 0.6 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Startup model | Type of model: INSILICO MODEL |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 332360 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |