+Open data
-Basic information
Entry | Database: PDB / ID: 1a0o | ||||||
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Title | CHEY-BINDING DOMAIN OF CHEA IN COMPLEX WITH CHEY | ||||||
Components |
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Keywords | CHEMOTAXIS / BACTERIAL CHEMOTAXIS / SIGNAL TRANSDUCTION / TWO-COMPONENT SYSTEM / HISTIDINE KINASE / RESPONSE REGULATOR | ||||||
Function / homology | Function and homology information negative regulation of protein modification process / methyl accepting chemotaxis protein complex / positive regulation of post-translational protein modification / 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 / protein histidine kinase activity / bacterial-type flagellum ...negative regulation of protein modification process / methyl accepting chemotaxis protein complex / positive regulation of post-translational protein modification / 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 / protein histidine kinase activity / bacterial-type flagellum / regulation of chemotaxis / thermotaxis / internal peptidyl-lysine acetylation / phosphorelay response regulator activity / protein acetylation / histidine kinase / phosphorelay sensor kinase activity / acetyltransferase activity / phosphorelay signal transduction system / establishment of localization in cell / chemotaxis / magnesium ion binding / signal transduction / ATP binding / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MIRAS, DENSITY MODIFICATION, MOLECULAR REPLACEMENT / Resolution: 2.95 Å | ||||||
Authors | Chinardet, N. / Welch, M. / Mourey, L. / Birck, C. / Samama, J.P. | ||||||
Citation | Journal: Nat.Struct.Biol. / Year: 1998 Title: Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY. Authors: Welch, M. / Chinardet, N. / Mourey, L. / Birck, C. / Samama, J.P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1a0o.cif.gz | 147.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1a0o.ent.gz | 116.8 KB | Display | PDB format |
PDBx/mmJSON format | 1a0o.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1a0o_validation.pdf.gz | 483.9 KB | Display | wwPDB validaton report |
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Full document | 1a0o_full_validation.pdf.gz | 502.7 KB | Display | |
Data in XML | 1a0o_validation.xml.gz | 29.4 KB | Display | |
Data in CIF | 1a0o_validation.cif.gz | 39.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/a0/1a0o ftp://data.pdbj.org/pub/pdb/validation_reports/a0/1a0o | HTTPS FTP |
-Related structure data
Related structure data | 1chnS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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2 |
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3 |
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4 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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-Components
#1: Protein | Mass: 13981.136 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Cellular location: CYTOPLASM / Production host: Escherichia coli (E. coli) / References: UniProt: P06143, UniProt: P0AE67*PLUS #2: Protein | Mass: 14505.375 Da / Num. of mol.: 4 / Fragment: CHEA 124-257 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Cellular location: CYTOPLASM / Production host: Escherichia coli (E. coli) References: UniProt: P07363, Transferases; Transferring phosphorus-containing groups; Phosphotransferases with a nitrogenous group as acceptor #3: Chemical | ChemComp-MN / |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 2 |
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-Sample preparation
Crystal | Density Matthews: 2.28 Å3/Da / Density % sol: 44 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 5.5 Details: PROTEIN WAS CRYSTALLIZED FROM 20% PEG MME 5K, 0.1 M MALONIC ACID, 0.1 M MES BUFFER PH 5.5, 0.02 M DTT, 0.01 M MANGANESE CHLORIDE | ||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / pH: 7.9 / Method: vapor diffusion / Details: drop was mixed with an equal volume of reservoir | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: SYNCHROTRON / Site: LURE / Beamline: DW32 / Wavelength: 0.97 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Mar 1, 1996 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97 Å / Relative weight: 1 |
Reflection | Resolution: 2.95→29 Å / Num. obs: 41612 / % possible obs: 92 % / Redundancy: 2.5 % / Rmerge(I) obs: 0.054 / Net I/σ(I): 9.5 |
Reflection shell | Resolution: 2.95→3.03 Å / Redundancy: 2.1 % / Rmerge(I) obs: 0.099 / Mean I/σ(I) obs: 6.8 / % possible all: 86.4 |
Reflection shell | *PLUS % possible obs: 86.4 % |
-Processing
Software |
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Refinement | Method to determine structure: MIRAS, DENSITY MODIFICATION, MOLECULAR REPLACEMENT Starting model: 1CHN Resolution: 2.95→27 Å / Rfactor Rfree error: 0.0072 / Data cutoff high absF: 100000 / Data cutoff low absF: 0.1 / Cross valid method: THROUGHOUT / σ(F): 0 Details: NCS CONSTRAINTS WERE ONLY APPLIED IN THE FIRST REFINEMENT CYCLES ONE OF THE CONSTRUCTS USED FOR THE CRYSTAL STRUCTURE DETERMINATION CONSISTS OF THE CHEY-BINDING DOMAIN OF CHEA FLANKED BY ...Details: NCS CONSTRAINTS WERE ONLY APPLIED IN THE FIRST REFINEMENT CYCLES ONE OF THE CONSTRUCTS USED FOR THE CRYSTAL STRUCTURE DETERMINATION CONSISTS OF THE CHEY-BINDING DOMAIN OF CHEA FLANKED BY DOMAIN LINKERS (CHEA124-257). IN THE FINAL MODEL, EACH MOLECULE OF THE COMPLEX COMPRISES 128 RESIDUES IN CHEY AND AN ACTIVE SITE-BOUND MN2+, AND 70 RESIDUES IN CHEA124-257 SPANNING THE REGION 159-228. NO ELECTRON DENSITY COULD BE ASSIGNED TO THE REMAINING RESIDUES IN CHEA124-257.
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Displacement parameters | Biso mean: 33.1 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.95→27 Å
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Refine LS restraints |
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Refine LS restraints NCS | NCS model details: UNRESTRAINED | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 2.95→3.08 Å / Rfactor Rfree error: 0.032 / Total num. of bins used: 8
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Xplor file |
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Software | *PLUS Name: X-PLOR / Version: 3.1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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