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Yorodumi- PDB-1udr: CHEY MUTANT WITH LYS 91 REPLACED BY ASP, LYS 92 REPLACED BY ALA, ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1udr | ||||||
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Title | CHEY MUTANT WITH LYS 91 REPLACED BY ASP, LYS 92 REPLACED BY ALA, ILE 96 REPLACED BY LYS AND ALA 98 REPLACED BY LEU (STABILIZING MUTATIONS IN HELIX 4) | ||||||
Components | CHEY PROTEIN | ||||||
Keywords | CHEMOTAXIS / PHOSPHORYL TRANSFER / SIGNAL TRANSDUCTION | ||||||
Function / homology | Function and homology information bacterial-type flagellum basal body, C ring / bacterial-type flagellum rotor complex / bacterial-type flagellum-dependent swimming motility / regulation of bacterial-type flagellum-dependent cell motility / aerotaxis / bacterial-type flagellum / regulation of chemotaxis / thermotaxis / internal peptidyl-lysine acetylation / phosphorelay response regulator activity ...bacterial-type flagellum basal body, C ring / bacterial-type flagellum rotor complex / bacterial-type flagellum-dependent swimming motility / regulation of bacterial-type flagellum-dependent cell motility / aerotaxis / bacterial-type flagellum / regulation of chemotaxis / thermotaxis / internal peptidyl-lysine acetylation / phosphorelay response regulator activity / protein acetylation / acetyltransferase activity / phosphorelay signal transduction system / chemotaxis / magnesium ion binding / signal transduction / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.9 Å | ||||||
Authors | Parraga, A. / Coll, M. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2000 Title: Towards understanding a molecular switch mechanism: thermodynamic and crystallographic studies of the signal transduction protein CheY. Authors: Sola, M. / Lopez-Hernandez, E. / Cronet, P. / Lacroix, E. / Serrano, L. / Coll, M. / Parraga, A. #1: Journal: J.Mol.Biol. / Year: 1996 Title: The Three-Dimensional Structure of Two Mutants of the Signal Transduction Protein Chey Suggest its Molecular Activation Mechanism Authors: Bellsolell, L. / Cronet, P. / Majolero, M. / Serrano, L. / Coll, M. #2: Journal: J.Mol.Biol. / Year: 1994 Title: Magnesium Binding to the Bacterial Chemotaxis Protein Chey Results in Large Conformational Changes Involving its Functional Surface Authors: Bellsolell, L. / Prieto, J. / Serrano, L. / Coll, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1udr.cif.gz | 105.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1udr.ent.gz | 85.9 KB | Display | PDB format |
PDBx/mmJSON format | 1udr.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ud/1udr ftp://data.pdbj.org/pub/pdb/validation_reports/ud/1udr | HTTPS FTP |
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-Related structure data
Related structure data | 1e6kC 1e6lC 1e6mC 3chyS S: Starting model for refinement 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
#1: Protein | Mass: 14184.355 Da / Num. of mol.: 4 / Mutation: K91D, K92A, I96K, A98L Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Plasmid: VECTOR PBAT DERIVED FROM PTZ18U (PHARMACIA) / Production host: Escherichia coli (E. coli) / References: UniProt: P06143, UniProt: P0AE67*PLUS #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: 2.62 Å3/Da / Density % sol: 54 % | ||||||||||||||||||||||||||||||
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Crystal | *PLUS | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / pH: 8.5 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: MARRESEARCH / Detector: IMAGE PLATE |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 42474 / % possible obs: 82.9 % / Observed criterion σ(I): 2 / Rmerge(I) obs: 0.058 |
Reflection | *PLUS Highest resolution: 1.9 Å / % possible obs: 87.2 % / Observed criterion σ(F): 2 / Rmerge(I) obs: 0.077 |
Reflection shell | *PLUS Highest resolution: 1.9 Å / Lowest resolution: 1.94 Å / % possible obs: 82.5 % |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 3CHY Resolution: 1.9→8 Å / σ(F): 2 /
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Refinement step | Cycle: LAST / Resolution: 1.9→8 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor Rfree: 0.222 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |