+Open data
-Basic information
Entry | Database: PDB / ID: 1c4w | ||||||
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Title | 1.9 A STRUCTURE OF A-THIOPHOSPHONATE MODIFIED CHEY D57C | ||||||
Components | CHEMOTAXIS PROTEIN CHEY | ||||||
Keywords | SIGNALING PROTEIN / Phosphono-CheY / Active Form of the Response Regulator / Chemotaxis | ||||||
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 / SYNCHROTRON / Resolution: 1.84 Å | ||||||
Authors | Halkides, C.J. / McEvoy, M.M. / Matsumura, P. / Volz, K. / Dahlquist, F.W. | ||||||
Citation | Journal: Biochemistry / Year: 2000 Title: The 1.9 A resolution crystal structure of phosphono-CheY, an analogue of the active form of the response regulator, CheY. Authors: Halkides, C.J. / McEvoy, M.M. / Casper, E. / Matsumura, P. / Volz, K. / Dahlquist, F.W. #1: Journal: Biochemistry / Year: 1998 Title: Synthesis and Biochemical Characterization of an Analogue of CheY-phosphate, a Signal Transduction Protein in Bacterial Chemotaxis Authors: Halkides, C.J. / Zhu, X. / Phillion, D.P. / Matsumura, P. / Dahlquist, F.W. #2: Journal: J.Biol.Chem. / Year: 1997 Title: Uncoupled Phosphorylation and Activation in Bacterial Chemotaxis: the 2.3 A Structure of an Aspartate to Lysine Mutant at Position 13 of CheY Authors: Jiang, M. / Bourret, R.B. / Simon, M.I. / Volz, K. #3: Journal: J.Biol.Chem. / Year: 1997 Title: Crystal Structures of CheY Mutants Y106W and T87I/Y106W. CheY Activation Correlates with Movement of Residue 106. Authors: Zhu, X. / Rebello, J. / Matsumura, P. / Volz, K. #4: Journal: J.Bacteriol. / Year: 1996 Title: Tyrosine 106 Plays an Important Role in Chemotaxis Signal Transduction in Escherichia Coli Authors: Zhu, X.Y. / Amsler, C.D. / Volz, K. / Matsumura, P. #5: Journal: J.Biol.Chem. / Year: 1995 Title: Uncoupled Phosphorylation and Activation in Bacterial Chemotaxis. The 2.1 A Structure of a Threonine to Isoleucine Mutant at Position 87 of CheY Authors: Ganguli, S. / Wang, H. / Matsumura, P. / Volz, K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1c4w.cif.gz | 40.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1c4w.ent.gz | 27.9 KB | Display | PDB format |
PDBx/mmJSON format | 1c4w.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/c4/1c4w ftp://data.pdbj.org/pub/pdb/validation_reports/c4/1c4w | HTTPS FTP |
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-Related structure data
Related structure data | |
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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: 14063.198 Da / Num. of mol.: 1 / Mutation: D57(CYQ) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Plasmid: PRL22 / Production host: Escherichia coli (E. coli) / References: UniProt: P06143, UniProt: P0AE67*PLUS |
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#2: 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: 2.06 Å3/Da / Density % sol: 40.19 % | ||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6.9 Details: PEG 6000, SODIUM ACETATE, PIPES, pH 6.9, VAPOR DIFFUSION/HANGING DROP, temperature 298K | ||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SSRL / Beamline: BL9-1 / Wavelength: 0.98 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: May 10, 1997 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.98 Å / Relative weight: 1 |
Reflection | Resolution: 1.84→50 Å / Num. all: 10492 / Observed criterion σ(I): 1 / Redundancy: 8 % / Rmerge(I) obs: 0.074 |
Reflection shell | Resolution: 1.85→1.96 Å / % possible all: 94.1 |
Reflection | *PLUS Num. obs: 10492 / Num. measured all: 84092 |
-Processing
Software |
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Refinement | Resolution: 1.84→10 Å / σ(F): 2 Details: THE ALPHA-THIOPHOSPHONATE GROUP COVALENTLY BOUND TO RESIDUE 57 WAS NOT INCLUDED IN THE REFINEMENT. RESIDUE 57 WAS REFINED AS AN ALANINE.
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Refinement step | Cycle: LAST / Resolution: 1.84→10 Å
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Refine LS restraints |
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Software | *PLUS Name: PROTIN/PROFFT / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 10 Å / σ(F): 2 / Rfactor obs: 0.208 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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