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Yorodumi- PDB-3dl8: Structure of the complex of aquifex aeolicus SecYEG and bacillus ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3dl8 | ||||||
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Title | Structure of the complex of aquifex aeolicus SecYEG and bacillus subtilis SecA | ||||||
Components |
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Keywords | PROTEIN TRANSPORT / RecA-type ATPase membrane protein translocation Protein-protein complex / ATP-binding / Cell membrane / Membrane / Metal-binding / Nucleotide-binding / Translocation / Transport / Transmembrane | ||||||
Function / homology | Function and homology information cell envelope Sec protein transport complex / protein-exporting ATPase activity / protein-secreting ATPase / protein transport by the Sec complex / intracellular protein transmembrane transport / protein-transporting ATPase activity / protein import / SRP-dependent cotranslational protein targeting to membrane, translocation / signal sequence binding / plasma membrane => GO:0005886 ...cell envelope Sec protein transport complex / protein-exporting ATPase activity / protein-secreting ATPase / protein transport by the Sec complex / intracellular protein transmembrane transport / protein-transporting ATPase activity / protein import / SRP-dependent cotranslational protein targeting to membrane, translocation / signal sequence binding / plasma membrane => GO:0005886 / protein transmembrane transporter activity / protein secretion / protein targeting / membrane => GO:0016020 / membrane raft / ATP binding / metal ion binding / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | Bacillus subtilis (bacteria) Aquifex aeolicus (bacteria) Aquifex Aeolicus (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 7.5 Å | ||||||
Authors | Nam, Y. / Zimmer, J. / Rapoport, T.A. | ||||||
Citation | Journal: Nature / Year: 2008 Title: Structure of a complex of the ATPase SecA and the protein-translocation channel. Authors: Zimmer, J. / Nam, Y. / Rapoport, T.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3dl8.cif.gz | 350.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3dl8.ent.gz | 211.8 KB | Display | PDB format |
PDBx/mmJSON format | 3dl8.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/dl/3dl8 ftp://data.pdbj.org/pub/pdb/validation_reports/dl/3dl8 | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 88803.023 Da / Num. of mol.: 2 / Fragment: UNP residues 1-779 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bacillus subtilis (bacteria) / Gene: secA, div+, BSU35300 / Production host: Escherichia coli (E. coli) / References: UniProt: P28366 #2: Protein | Mass: 48139.977 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Aquifex aeolicus (bacteria) / Gene: secY, aq_079 / Production host: Escherichia coli (E. coli) / References: UniProt: O66491 #3: Protein | Mass: 7504.100 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Aquifex Aeolicus (bacteria) / Production host: Escherichia coli (E. coli) / References: UniProt: D0VWU4*PLUS #4: Protein | Mass: 11358.197 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Aquifex aeolicus (bacteria) / Gene: secG, aq_098 / Production host: Escherichia coli (E. coli) / References: UniProt: O66505 |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.7 Å3/Da / Density % sol: 67.88 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 26-28% (w/v) PEG 3350 and 250mM lithium sulfate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 200 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 0.979 Å |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Dec 23, 2007 |
Radiation | Monochromator: graphite / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.979 Å / Relative weight: 1 |
Reflection | Resolution: 7.5→15 Å / Num. all: 5443 / Num. obs: 5416 / % possible obs: 99.5 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 |
Reflection shell | Resolution: 7.5→7.9 Å / % possible all: 99 |
-Processing
Software |
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Refinement | Resolution: 7.5→14.99 Å / Rfactor Rfree error: 0.017 / Occupancy max: 1 / Occupancy min: 1 / Data cutoff high absF: 3033230 / Data cutoff low absF: 0 / Isotropic thermal model: OVERALL / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber Details: BULK SOLVENT MODEL USED. MODEL CONTAINS BACKBONE ONLY.
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 234.636 Å2 / ksol: 0.25 e/Å3 | ||||||||||||||||||||||||||||
Displacement parameters | Biso max: 580.7 Å2 / Biso mean: 401.742 Å2 / Biso min: 229.26 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 7.5→14.99 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 7.5→7.9 Å / Rfactor Rfree error: 0.055 / Total num. of bins used: 6
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Xplor file |
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