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Yorodumi- PDB-1txq: Crystal structure of the EB1 C-terminal domain complexed with the... -
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-Basic information
Entry | Database: PDB / ID: 1txq | ||||||
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Title | Crystal structure of the EB1 C-terminal domain complexed with the CAP-Gly domain of p150Glued | ||||||
Components |
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Keywords | STRUCTURAL PROTEIN/PROTEIN BINDING / PROTEIN COMPLEX / STRUCTURAL PROTEIN-PROTEIN BINDING COMPLEX | ||||||
Function / homology | Function and homology information positive regulation of neuromuscular junction development / centriolar subdistal appendage / cell cortex region / protein localization to astral microtubule / cortical microtubule cytoskeleton / centriole-centriole cohesion / mitotic spindle astral microtubule end / ventral spinal cord development / microtubule anchoring at centrosome / maintenance of synapse structure ...positive regulation of neuromuscular junction development / centriolar subdistal appendage / cell cortex region / protein localization to astral microtubule / cortical microtubule cytoskeleton / centriole-centriole cohesion / mitotic spindle astral microtubule end / ventral spinal cord development / microtubule anchoring at centrosome / maintenance of synapse structure / melanosome transport / protein localization to microtubule / nuclear membrane disassembly / microtubule plus-end / positive regulation of microtubule nucleation / cell projection membrane / XBP1(S) activates chaperone genes / attachment of mitotic spindle microtubules to kinetochore / dynein complex / COPI-independent Golgi-to-ER retrograde traffic / microtubule plus-end binding / non-motile cilium assembly / microtubule bundle formation / retrograde transport, endosome to Golgi / nuclear migration / protein localization to centrosome / microtubule associated complex / motor behavior / microtubule organizing center / neuromuscular process / negative regulation of microtubule polymerization / neuromuscular junction development / intercellular bridge / mitotic spindle pole / microtubule polymerization / cell leading edge / establishment of mitotic spindle orientation / Signaling by ALK fusions and activated point mutants / spindle assembly / regulation of microtubule polymerization or depolymerization / spindle midzone / cytoplasmic microtubule / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / COPI-mediated anterograde transport / Mitotic Prometaphase / regulation of mitotic spindle organization / EML4 and NUDC in mitotic spindle formation / positive regulation of microtubule polymerization / Loss of Nlp from mitotic centrosomes / Loss of proteins required for interphase microtubule organization from the centrosome / Recruitment of mitotic centrosome proteins and complexes / Resolution of Sister Chromatid Cohesion / Recruitment of NuMA to mitotic centrosomes / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / Anchoring of the basal body to the plasma membrane / MHC class II antigen presentation / neuron projection maintenance / centriole / tubulin binding / AURKA Activation by TPX2 / ciliary basal body / RHO GTPases Activate Formins / tau protein binding / protein localization / mitotic spindle / spindle / kinetochore / spindle pole / neuron cellular homeostasis / Separation of Sister Chromatids / The role of GTSE1 in G2/M progression after G2 checkpoint / microtubule cytoskeleton / Regulation of PLK1 Activity at G2/M Transition / cell migration / mitotic cell cycle / nuclear envelope / nervous system development / cell cortex / microtubule binding / microtubule / molecular adaptor activity / neuron projection / cadherin binding / cell division / axon / focal adhesion / centrosome / neuronal cell body / protein kinase binding / Golgi apparatus / RNA binding / membrane / identical protein binding / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 1.8 Å | ||||||
Authors | Hayashi, I. / Ikura, M. | ||||||
Citation | Journal: Mol.Cell / Year: 2005 Title: Structural Basis for the Activation of Microtubule Assembly by the EB1 and p150(Glued) Complex Authors: Hayashi, I. / Wilde, A. / Mal, T.K. / Ikura, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1txq.cif.gz | 42 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1txq.ent.gz | 28.9 KB | Display | PDB format |
PDBx/mmJSON format | 1txq.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/tx/1txq ftp://data.pdbj.org/pub/pdb/validation_reports/tx/1txq | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Components on special symmetry positions |
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Details | The biological assembly is a hetero-tetramer. |
-Components
#1: Protein | Mass: 9928.076 Da / Num. of mol.: 1 / Fragment: p150Glued CAP-Gly domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: p150Glued / Plasmid: pET15b / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: Q14203 |
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#2: Protein | Mass: 9778.598 Da / Num. of mol.: 1 / Fragment: EB1 C-terminal domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: EB1 / Plasmid: pGEX4T-1 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: Q15691 |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.01 Å3/Da / Density % sol: 38.8 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, sitting drop / pH: 6.5 Details: ammonium sulphate, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 19-BM / Wavelength: 0.9513 Å |
Detector | Detector: CCD / Date: Jul 10, 2003 |
Radiation | Monochromator: SAGITALLY FOCUSED Si(111) / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9513 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→50 Å / Num. obs: 14411 / % possible obs: 99.9 % / Observed criterion σ(F): 2 / Biso Wilson estimate: 22.7 Å2 |
Reflection shell | Resolution: 1.8→1.91 Å / % possible all: 99.5 |
-Processing
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Refinement | Method to determine structure: MAD / Resolution: 1.8→17.93 Å / Rfactor Rfree error: 0.007 / Data cutoff high absF: 769082.92 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 47.5391 Å2 / ksol: 0.433519 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 32 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 1.8→17.93 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.8→1.91 Å / Rfactor Rfree error: 0.021 / Total num. of bins used: 6
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Xplor file |
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