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Yorodumi- PDB-2qi9: ABC-transporter BtuCD in complex with its periplasmic binding pro... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2qi9 | ||||||
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Title | ABC-transporter BtuCD in complex with its periplasmic binding protein BtuF | ||||||
Components |
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Keywords | MEMBRANE PROTEIN / Inner membrane / Membrane / Transmembrane / Transport / ATP-binding / Hydrolase / Nucleotide-binding / Periplasm | ||||||
Function / homology | Function and homology information ABC-type vitamin B12 transporter / BtuCD complex / cobalamin transport complex / ABC-type vitamin B12 transporter activity / cobalamin transport / cobalamin binding / extrinsic component of membrane / transmembrane transporter activity / ATPase-coupled transmembrane transporter activity / ATP-binding cassette (ABC) transporter complex ...ABC-type vitamin B12 transporter / BtuCD complex / cobalamin transport complex / ABC-type vitamin B12 transporter activity / cobalamin transport / cobalamin binding / extrinsic component of membrane / transmembrane transporter activity / ATPase-coupled transmembrane transporter activity / ATP-binding cassette (ABC) transporter complex / outer membrane-bounded periplasmic space / periplasmic space / ATP hydrolysis activity / ATP binding / membrane / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2.6 Å | ||||||
Authors | Hvorup, R.N. / Goetz, B.A. / Niederer, M. / Hollenstein, K. / Perozo, E. / Locher, K.P. | ||||||
Citation | Journal: Science / Year: 2007 Title: Asymmetry in the structure of the ABC transporter-binding protein complex BtuCD-BtuF. Authors: Hvorup, R.N. / Goetz, B.A. / Niederer, M. / Hollenstein, K. / Perozo, E. / Locher, K.P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2qi9.cif.gz | 245.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2qi9.ent.gz | 209.8 KB | Display | PDB format |
PDBx/mmJSON format | 2qi9.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qi/2qi9 ftp://data.pdbj.org/pub/pdb/validation_reports/qi/2qi9 | HTTPS FTP |
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-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
-Vitamin B12 import ... , 2 types, 4 molecules ABCD
#1: Protein | Mass: 35375.488 Da / Num. of mol.: 2 / Mutation: C18S, C32S, C120S, C156S, C205S, C206S, C267S Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Gene: btuC / Plasmid: pET19b / Production host: Escherichia coli (E. coli) / References: UniProt: P06609 #2: Protein | Mass: 27520.170 Da / Num. of mol.: 2 / Mutation: C180S Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Gene: btuD / Plasmid: pET19b / Production host: Escherichia coli (E. coli) / References: UniProt: P06611, EC: 3.6.3.33 |
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-Protein , 1 types, 1 molecules F
#3: Protein | Mass: 27140.604 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Gene: btuF / Plasmid: pET19b / Production host: Escherichia coli (E. coli) / References: UniProt: P37028 |
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-Non-polymers , 5 types, 30 molecules
#4: Chemical | #5: Chemical | ChemComp-SO4 / #6: Chemical | #7: Chemical | ChemComp-PEG / #8: Water | ChemComp-HOH / | |
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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: 4 Å3/Da / Density % sol: 69.26 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 8.4 Details: 30-38% (w/v) polyethylene glycol 400, 50mM either of Tris‑HCl pH 8.4 or Glycine-NaOH pH 9.4 and 400mM (NH4)2SO4., VAPOR DIFFUSION, SITTING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K | ||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 0.93209, 0.97934, 0.97980 | ||||||||||||
Detector | Date: Feb 18, 2007 | ||||||||||||
Radiation | Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||
Radiation wavelength |
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Reflection | Resolution: 2.586→29.814 Å / Num. all: 74391 / Num. obs: 74100 / % possible obs: 100 % / Redundancy: 4.7 % / Rmerge(I) obs: 0.074 / Rsym value: 0.074 | ||||||||||||
Reflection shell | Resolution: 2.6→2.69 Å / Redundancy: 4.7 % / Rmerge(I) obs: 0.57 / Rsym value: 0.57 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 2.6→29.814 Å / σ(F): 0
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Solvent computation | Bsol: 48.132 Å2 | ||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 84.616 Å2
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Refinement step | Cycle: LAST / Resolution: 2.6→29.814 Å
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Xplor file |
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