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Yorodumi- PDB-1uk5: Solution structure of the Murine BAG domain of Bcl2-associated at... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1uk5 | ||||||
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Title | Solution structure of the Murine BAG domain of Bcl2-associated athanogene 3 | ||||||
Components | BAG-family molecular chaperone regulator-3 | ||||||
Keywords | CHAPERONE / Triple Helix Bandle / CAIR-1 / Bis / RIKEN Structural Genomics/Proteomics Initiative / RSGI / Structural Genomics | ||||||
Function / homology | Function and homology information : / Regulation of HSF1-mediated heat shock response / negative regulation of striated muscle cell apoptotic process / negative regulation of protein targeting to mitochondrion / adenyl-nucleotide exchange factor activity / protein folding chaperone complex / positive regulation of aggrephagy / muscle cell cellular homeostasis / chaperone-mediated autophagy / spinal cord development ...: / Regulation of HSF1-mediated heat shock response / negative regulation of striated muscle cell apoptotic process / negative regulation of protein targeting to mitochondrion / adenyl-nucleotide exchange factor activity / protein folding chaperone complex / positive regulation of aggrephagy / muscle cell cellular homeostasis / chaperone-mediated autophagy / spinal cord development / autophagosome assembly / extrinsic apoptotic signaling pathway via death domain receptors / cellular response to unfolded protein / stress fiber / extrinsic apoptotic signaling pathway in absence of ligand / positive regulation of protein export from nucleus / brain development / Z disc / positive regulation of protein import into nucleus / cellular response to mechanical stimulus / cellular response to heat / protein-folding chaperone binding / protein stabilization / neuron projection / protein-containing complex binding / negative regulation of apoptotic process / nucleus / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | SOLUTION NMR | ||||||
Authors | Hatta, R. / Yoshida, M. / Hayashi, F. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: Structure / Year: 2010 Title: The C-terminal BAG domain of BAG5 induces conformational changes of the Hsp70 nucleotide-binding domain for ADP-ATP exchange Authors: Arakawa, A. / Handa, N. / Ohsawa, N. / Shida, M. / Kigawa, T. / Hayashi, F. / Shirouzu, M. / Yokoyama, S. | ||||||
History |
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Remark 650 | HELIX DETERMINATION METHOD: AUTHOR DETERMINED |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1uk5.cif.gz | 653.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1uk5.ent.gz | 546.5 KB | Display | PDB format |
PDBx/mmJSON format | 1uk5.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/uk/1uk5 ftp://data.pdbj.org/pub/pdb/validation_reports/uk/1uk5 | HTTPS FTP |
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-Related structure data
Related structure data | 1ugoC 2d9dC 3a8yC C: citing same article (ref.) |
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Similar structure data | |
Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 11832.287 Da / Num. of mol.: 1 / Fragment: BAG domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: FANTOM 2 cDNA 4931440G06 / Plasmid: P020122-09 / Production host: Cell-free synthesis (others) / References: UniProt: Q9JLV1 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 0.7mM 13C, 15N-labeled protein, 20mM phosphate buffer, 90mM NaCl, 40mM MgSO4, 0.4mM NaN3, 8% D2O Solvent system: 92% H2O, 8% D2O |
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Sample conditions | Ionic strength: 250mM / pH: 6.5 / Pressure: ambient / Temperature: 298 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 800 MHz |
-Processing
NMR software |
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NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations, target function Conformers calculated total number: 100 / Conformers submitted total number: 20 |