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- PDB-9m1m: Cryo-EM structure of the TBC-DEC-Arl2-alpha-beta-tubulin complex ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 9m1m | ||||||
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Title | Cryo-EM structure of the TBC-DEC-Arl2-alpha-beta-tubulin complex with GDP-AlFx | ||||||
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![]() | CHAPERONE / complex | ||||||
Function / homology | ![]() peripheral nervous system neuron axonogenesis / Transport of nucleosides and free purine and pyrimidine bases across the plasma membrane / post-chaperonin tubulin folding pathway / muscle atrophy / cell morphogenesis involved in neuron differentiation / Regulation of PLK1 Activity at G2/M Transition / Loss of Nlp from mitotic centrosomes / Loss of proteins required for interphase microtubule organization from the centrosome / Anchoring of the basal body to the plasma membrane / AURKA Activation by TPX2 ...peripheral nervous system neuron axonogenesis / Transport of nucleosides and free purine and pyrimidine bases across the plasma membrane / post-chaperonin tubulin folding pathway / muscle atrophy / cell morphogenesis involved in neuron differentiation / Regulation of PLK1 Activity at G2/M Transition / Loss of Nlp from mitotic centrosomes / Loss of proteins required for interphase microtubule organization from the centrosome / Anchoring of the basal body to the plasma membrane / AURKA Activation by TPX2 / Recruitment of mitotic centrosome proteins and complexes / odontoblast differentiation / photoreceptor connecting cilium / Post-chaperonin tubulin folding pathway / negative regulation of GTPase activity / tubulin complex assembly / bicellular tight junction assembly / Neutrophil degranulation / maintenance of protein location in nucleus / Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane / Resolution of Sister Chromatid Cohesion / Hedgehog 'off' state / Cilium Assembly / Intraflagellar transport / COPI-dependent Golgi-to-ER retrograde traffic / Mitotic Prometaphase / Carboxyterminal post-translational modifications of tubulin / RHOH GTPase cycle / EML4 and NUDC in mitotic spindle formation / Sealing of the nuclear envelope (NE) by ESCRT-III / Kinesins / PKR-mediated signaling / Separation of Sister Chromatids / The role of GTSE1 in G2/M progression after G2 checkpoint / Aggrephagy / adherens junction assembly / centrosome cycle / RHO GTPases activate IQGAPs / RHO GTPases Activate Formins / positive regulation of cell-substrate adhesion / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / MHC class II antigen presentation / Recruitment of NuMA to mitotic centrosomes / regulation of glycolytic process / COPI-mediated anterograde transport / regulation of aerobic respiration / negative regulation of microtubule polymerization / regulation of synapse organization / nuclear envelope lumen / MHC class I protein binding / regulation of microtubule polymerization / lateral plasma membrane / developmental growth / negative regulation of cell-substrate adhesion / bicellular tight junction / alpha-tubulin binding / beta-tubulin binding / intercellular bridge / spindle assembly / positive regulation of microtubule polymerization / tubulin binding / GTPase activator activity / adult locomotory behavior / mitotic spindle organization / post-embryonic development / adherens junction / structural constituent of cytoskeleton / mitochondrial intermembrane space / microtubule cytoskeleton organization / cytoplasmic ribonucleoprotein granule / RAS processing / mitotic spindle / GDP binding / protein folding / mitotic cell cycle / protein-folding chaperone binding / microtubule cytoskeleton / cell body / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / microtubule / cytoskeleton / ciliary basal body / mitochondrial matrix / GTPase activity / ubiquitin protein ligase binding / centrosome / GTP binding / nucleolus / endoplasmic reticulum / mitochondrion / nucleoplasm / metal ion binding / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.21 Å | ||||||
![]() | Seong, Y.J. / Kim, H.M. / Byun, K.M. / Park, Y.W. / Roh, S.H. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Structural dissection of alpha beta-tubulin heterodimer assembly and disassembly by human tubulin-specific chaperones Authors: Seong, Y.J. / Kim, H.M. / Byun, K.M. / Park, Y.W. / Roh, S.H. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 570.7 KB | Display | ![]() |
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PDB format | ![]() | 450.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.1 MB | Display | ![]() |
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Full document | ![]() | 1.1 MB | Display | |
Data in XML | ![]() | 72.6 KB | Display | |
Data in CIF | ![]() | 114.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 63576MC ![]() 9m1iC ![]() 9m1jC ![]() 9m1kC ![]() 9m1lC ![]() 9m1nC C: citing same article ( M: map data used to model this data |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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Components
-Tubulin-specific chaperone ... , 3 types, 3 molecules CDE
#1: Protein | Mass: 39300.125 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#2: Protein | Mass: 132752.516 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
#3: Protein | Mass: 59422.020 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
-Protein , 3 types, 3 molecules Gab
#4: Protein | Mass: 20903.992 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#5: Protein | Mass: 50204.445 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: Q2XVP4, Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement |
#6: Protein | Mass: 49717.629 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
-Non-polymers , 4 types, 7 molecules 






#7: Chemical | ChemComp-GDP / | ||
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#8: Chemical | ChemComp-AF3 / | ||
#9: Chemical | #10: Chemical | |
-Details
Has ligand of interest | Y |
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Has protein modification | N |
-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
Component |
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Molecular weight | Value: 0.35 MDa / Experimental value: YES | ||||||||||||||||||||||||
Source (natural) |
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Source (recombinant) |
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Buffer solution | pH: 7 | ||||||||||||||||||||||||
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||
Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: TFS KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 800 nm |
Image recording | Electron dose: 50 e/Å2 / Film or detector model: TFS FALCON 4i (4k x 4k) |
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Processing
EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | |||||||||
3D reconstruction | Resolution: 2.21 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 729421 / Symmetry type: POINT |