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Yorodumi- PDB-1tyf: THE STRUCTURE OF CLPP AT 2.3 ANGSTROM RESOLUTION SUGGESTS A MODEL... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1tyf | ||||||
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Title | THE STRUCTURE OF CLPP AT 2.3 ANGSTROM RESOLUTION SUGGESTS A MODEL FOR ATP-DEPENDENT PROTEOLYSIS | ||||||
Components | CLP PEPTIDASE | ||||||
Keywords | PEPTIDASE | ||||||
Function / homology | Function and homology information HslUV protease complex / endopeptidase Clp / endopeptidase Clp complex / positive regulation of programmed cell death / response to temperature stimulus / ATP-dependent peptidase activity / protein quality control for misfolded or incompletely synthesized proteins / proteasomal protein catabolic process / serine-type peptidase activity / response to radiation ...HslUV protease complex / endopeptidase Clp / endopeptidase Clp complex / positive regulation of programmed cell death / response to temperature stimulus / ATP-dependent peptidase activity / protein quality control for misfolded or incompletely synthesized proteins / proteasomal protein catabolic process / serine-type peptidase activity / response to radiation / ATPase binding / response to heat / serine-type endopeptidase activity / proteolysis / identical protein binding / membrane / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.3 Å | ||||||
Authors | Wang, J. / Hartling, J.A. / Flanagan, J.M. | ||||||
Citation | Journal: Cell(Cambridge,Mass.) / Year: 1997 Title: The structure of ClpP at 2.3 A resolution suggests a model for ATP-dependent proteolysis. Authors: Wang, J. / Hartling, J.A. / Flanagan, J.M. #1: Journal: J.Biol.Chem. / Year: 1990 Title: Sequence and Structure of Clp P, the Proteolytic Component of the ATP-Dependent Clp Protease of Escherichia Coli Authors: Maurizi, M.R. / Clark, W.P. / Katayama, Y. / Rudikoff, S. / Pumphrey, J. / Bowers, B. / Gottesman, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1tyf.cif.gz | 511.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1tyf.ent.gz | 423.8 KB | Display | PDB format |
PDBx/mmJSON format | 1tyf.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1tyf_validation.pdf.gz | 554.3 KB | Display | wwPDB validaton report |
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Full document | 1tyf_full_validation.pdf.gz | 640.1 KB | Display | |
Data in XML | 1tyf_validation.xml.gz | 110.2 KB | Display | |
Data in CIF | 1tyf_validation.cif.gz | 152 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ty/1tyf ftp://data.pdbj.org/pub/pdb/validation_reports/ty/1tyf | HTTPS FTP |
-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
#1: Protein | Mass: 21586.863 Da / Num. of mol.: 14 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / References: UniProt: P0A6G7, endopeptidase Clp #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.55 Å3/Da / Density % sol: 55 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 7.5 / Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 110 K |
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Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X12C |
Detector | Detector: CCD / Date: Dec 1, 1995 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | % possible obs: 100 % / Redundancy: 5 % / Rmerge(I) obs: 0.077 |
Reflection | *PLUS Highest resolution: 2.2 Å / Lowest resolution: 80 Å / Num. obs: 142952 |
-Processing
Software |
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Refinement | Resolution: 2.3→80 Å / σ(F): 2
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Displacement parameters | Biso mean: 32 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.3→80 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |