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Yorodumi- PDB-2qwp: Crystal structure of disulfide-bond-crosslinked complex of bovine... -
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-Basic information
Entry | Database: PDB / ID: 2qwp | ||||||
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Title | Crystal structure of disulfide-bond-crosslinked complex of bovine hsc70 (1-394aa)R171C and bovine Auxilin (810-910aa)D876C in the ADP*Pi form #2 | ||||||
Components |
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Keywords | CHAPERONE / chaperone-cochaperone complex / ATP-binding / Nucleotide-binding / Nucleus / Phosphorylation / Stress response / Hydrolase / Protein phosphatase / SH3-binding | ||||||
Function / homology | Function and homology information regulation of clathrin coat assembly / Regulation of HSF1-mediated heat shock response / Attenuation phase / HSF1-dependent transactivation / Protein methylation / GABA synthesis, release, reuptake and degradation / PKR-mediated signaling / mRNA Splicing - Major Pathway / synaptic vesicle recycling / synaptic vesicle uncoating ...regulation of clathrin coat assembly / Regulation of HSF1-mediated heat shock response / Attenuation phase / HSF1-dependent transactivation / Protein methylation / GABA synthesis, release, reuptake and degradation / PKR-mediated signaling / mRNA Splicing - Major Pathway / synaptic vesicle recycling / synaptic vesicle uncoating / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / chaperone-mediated autophagy translocation complex disassembly / slow axonal transport / clathrin-uncoating ATPase activity / protein targeting to lysosome involved in chaperone-mediated autophagy / clathrin heavy chain binding / late endosomal microautophagy / AUF1 (hnRNP D0) binds and destabilizes mRNA / clathrin coat disassembly / Hydrolases; Acting on ester bonds; Phosphoric-monoester hydrolases / Clathrin-mediated endocytosis / clathrin-dependent endocytosis / Prp19 complex / presynaptic cytosol / Neutrophil degranulation / postsynaptic cytosol / clathrin-coated vesicle / clathrin binding / non-chaperonin molecular chaperone ATPase / chaperone cofactor-dependent protein refolding / intracellular transport / autophagosome / dephosphorylation / protein folding chaperone / heat shock protein binding / RNA splicing / protein tyrosine phosphatase activity / ATP-dependent protein folding chaperone / spliceosomal complex / terminal bouton / mRNA processing / SH3 domain binding / melanosome / protein-macromolecule adaptor activity / presynapse / protein refolding / vesicle / postsynaptic density / lysosome / molecular adaptor activity / ribonucleoprotein complex / lysosomal membrane / protein domain specific binding / intracellular membrane-bounded organelle / negative regulation of DNA-templated transcription / dendrite / nucleolus / ATP hydrolysis activity / ATP binding / nucleus / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | Bos taurus (cattle) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 1.75 Å | ||||||
Authors | Jiang, J. / Maes, E.G. / Wang, L. / Taylor, A.B. / Hinck, A.P. / Lafer, E.M. / Sousa, R. | ||||||
Citation | Journal: Mol.Cell / Year: 2007 Title: Structural basis of J cochaperone binding and regulation of Hsp70. Authors: Jiang, J. / Maes, E.G. / Taylor, A.B. / Wang, L. / Hinck, A.P. / Lafer, E.M. / Sousa, R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2qwp.cif.gz | 112.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2qwp.ent.gz | 88.3 KB | Display | PDB format |
PDBx/mmJSON format | 2qwp.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qw/2qwp ftp://data.pdbj.org/pub/pdb/validation_reports/qw/2qwp | HTTPS FTP |
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-Related structure data
Related structure data | 2qw9C 2qwlC 2qwmC 2qwnC 2qwoC 2qwqC 2qwrC C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
-Protein , 2 types, 2 molecules AB
#1: Protein | Mass: 43368.059 Da / Num. of mol.: 1 / Mutation: R171C Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bos taurus (cattle) / Gene: HSPA8, HSC70 / Plasmid: pRSET / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)pLysS / References: UniProt: P19120 |
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#2: Protein | Mass: 10747.485 Da / Num. of mol.: 1 / Mutation: D876C Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bos taurus (cattle) / Gene: DNAJC6 / Plasmid: pGEX4T1 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: Q27974, protein-tyrosine-phosphatase |
-Non-polymers , 7 types, 298 molecules
#3: Chemical | ChemComp-PO4 / | ||||||||||
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#4: Chemical | #5: Chemical | ChemComp-MG / | #6: Chemical | ChemComp-ADP / | #7: Chemical | ChemComp-ACY / | #8: Chemical | #9: 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: 2.36 Å3/Da / Density % sol: 47.92 % |
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Crystal grow | Temperature: 289 K / Method: microbatch under oil / pH: 8.5 Details: PEG3350, Ammonium Acetate, pH 8.5, microbatch under oil, temperature 289K |
-Data collection
Diffraction source | Source: SYNCHROTRON / Site: ALS / Beamline: 5.0.1 / Wavelength: 1 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Detector | Date: Feb 3, 2007 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 1.75→50 Å / Num. obs: 48554 / % possible obs: 91.2 % / Redundancy: 6 % / Rmerge(I) obs: 0.08 / Χ2: 1.069 / Net I/σ(I): 10.4 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell |
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-Phasing
Phasing | Method: molecular replacement |
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.75→40.66 Å / Cor.coef. Fo:Fc: 0.953 / Cor.coef. Fo:Fc free: 0.927 / SU B: 5.04 / SU ML: 0.095 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.138 / ESU R Free: 0.133 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 27.892 Å2
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Refinement step | Cycle: LAST / Resolution: 1.75→40.66 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.75→1.795 Å / Total num. of bins used: 20
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