+
Open data
-
Basic information
Entry | Database: PDB / ID: 3eab | ||||||
---|---|---|---|---|---|---|---|
Title | Crystal structure of Spastin MIT in complex with ESCRT III | ||||||
![]() |
| ||||||
![]() | CELL CYCLE / Spastin / CHMP / MIT / ESCRT / Alternative splicing / ATP-binding / Cytoplasm / Disease mutation / Hereditary spastic paraplegia / Nucleotide-binding / Nucleus / Polymorphism | ||||||
Function / homology | ![]() cytokinetic process / microtubule-severing ATPase / microtubule severing ATPase activity / microtubule severing / MIT domain binding / endoplasmic reticulum tubular network / positive regulation of microtubule depolymerization / amphisome membrane / multivesicular body-lysosome fusion / vesicle fusion with vacuole ...cytokinetic process / microtubule-severing ATPase / microtubule severing ATPase activity / microtubule severing / MIT domain binding / endoplasmic reticulum tubular network / positive regulation of microtubule depolymerization / amphisome membrane / multivesicular body-lysosome fusion / vesicle fusion with vacuole / ESCRT III complex disassembly / late endosome to lysosome transport / ESCRT III complex / kinetochore microtubule / endosome transport via multivesicular body sorting pathway / cytoskeleton-dependent cytokinesis / mitotic nuclear membrane reassembly / regulation of centrosome duplication / nuclear membrane reassembly / Sealing of the nuclear envelope (NE) by ESCRT-III / midbody abscission / vacuolar transport / multivesicular body sorting pathway / membrane coat / membrane fission / plasma membrane repair / late endosome to vacuole transport / multivesicular body membrane / ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway / multivesicular body assembly / regulation of mitotic spindle assembly / microtubule bundle formation / anterograde axonal transport / mitotic spindle disassembly / protein hexamerization / exit from mitosis / mitotic metaphase chromosome alignment / axonal transport of mitochondrion / nucleus organization / beta-tubulin binding / viral budding via host ESCRT complex / positive regulation of cytokinesis / autophagosome membrane / autophagosome maturation / mitotic cytokinesis / alpha-tubulin binding / endoplasmic reticulum to Golgi vesicle-mediated transport / metabolic process / nuclear pore / axon cytoplasm / isomerase activity / multivesicular body / lipid droplet / axonogenesis / viral budding from plasma membrane / establishment of protein localization / protein homooligomerization / kinetochore / autophagy / spindle pole / protein transport / late endosome membrane / midbody / cytoplasmic vesicle / microtubule binding / nuclear membrane / microtubule / endosome membrane / endosome / protein domain specific binding / cell division / lysosomal membrane / axon / centrosome / protein-containing complex binding / endoplasmic reticulum membrane / perinuclear region of cytoplasm / ATP hydrolysis activity / extracellular exosome / nucleoplasm / ATP binding / identical protein binding / nucleus / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Yang, D. / Rimanchi, N. / Renvoise, B. / Lippincott-Schwartz, J. / Blackstone, C. / Hurley, J.H. | ||||||
![]() | ![]() Title: Structural basis for midbody targeting of spastin by the ESCRT-III protein CHMP1B. Authors: Yang, D. / Rismanchi, N. / Renvoise, B. / Lippincott-Schwartz, J. / Blackstone, C. / Hurley, J.H. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 154 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 126.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 515 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 547.7 KB | Display | |
Data in XML | ![]() | 29.4 KB | Display | |
Data in CIF | ![]() | 40.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
---|
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| ||||||||
2 | ![]()
| ||||||||
3 | ![]()
| ||||||||
4 | ![]()
| ||||||||
5 | ![]()
| ||||||||
6 | ![]()
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 10314.937 Da / Num. of mol.: 6 / Fragment: UNP residues 112 to 196 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Protein/peptide | Mass: 5420.950 Da / Num. of mol.: 6 / Fragment: UNP residues 145 to 194 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 3.76 Å3/Da / Density % sol: 67.28 % |
---|---|
Crystal grow | Temperature: 288 K / Method: vapor diffusion, hanging drop / pH: 4.6 Details: 10% PEG 2000 MME, 0.2 M Ammonia Sulfate, 0.1 M Sodium Acetate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 288K |
-Data collection
Diffraction | Mean temperature: 100 K | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Diffraction source | Source: ![]() ![]() ![]() | ||||||||||||
Detector | Type: MAR scanner 300 mm plate / Detector: IMAGE PLATE / Date: Feb 4, 2008 | ||||||||||||
Radiation | Monochromator: Si 220 / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||
Radiation wavelength |
| ||||||||||||
Reflection | Resolution: 2.3→50 Å / Num. obs: 59615 / % possible obs: 90.9 % / Biso Wilson estimate: 24.5 Å2 | ||||||||||||
Reflection shell | Resolution: 2.3→2.38 Å / % possible all: 53.3 |
-
Processing
Software |
| |||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]()
| |||||||||||||||||||||||||
Solvent computation | Solvent model: FLAT MODEL / Bsol: 43.8832 Å2 / ksol: 0.345367 e/Å3 | |||||||||||||||||||||||||
Displacement parameters | Biso mean: 53.7 Å2
| |||||||||||||||||||||||||
Refine analyze |
| |||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.5→47.65 Å
| |||||||||||||||||||||||||
Refine LS restraints |
| |||||||||||||||||||||||||
LS refinement shell | Resolution: 2.5→2.66 Å / Rfactor Rfree error: 0.02 / Total num. of bins used: 6
| |||||||||||||||||||||||||
Xplor file |
|