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Yorodumi- PDB-2pfu: NMR structure determination of the periplasmic domain of ExbD fro... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2pfu | ||||||
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Title | NMR structure determination of the periplasmic domain of ExbD from E.coli | ||||||
Components | Biopolymer transport exbD protein | ||||||
Keywords | TRANSPORT PROTEIN / ExbD / TonB system / proton motive force / periplasmic domain | ||||||
Function / homology | Function and homology information energy transducer activity / bacteriocin transport / cobalamin transport / intracellular monoatomic cation homeostasis / plasma membrane protein complex / transmembrane transporter complex / transmembrane transporter activity / cell outer membrane / protein transport / intracellular iron ion homeostasis ...energy transducer activity / bacteriocin transport / cobalamin transport / intracellular monoatomic cation homeostasis / plasma membrane protein complex / transmembrane transporter complex / transmembrane transporter activity / cell outer membrane / protein transport / intracellular iron ion homeostasis / protein stabilization / protein homodimerization activity / membrane / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Garcia-Herrero, A. / Peacock, S.R. / Howard, P.S. / Vogel, H.J. | ||||||
Citation | Journal: Mol.Microbiol. / Year: 2007 Title: The solution structure of the periplasmic domain of the TonB system ExbD protein reveals an unexpected structural homology with siderophore-binding proteins. Authors: Garcia-Herrero, A. / Peacock, R.S. / Howard, S.P. / Vogel, H.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2pfu.cif.gz | 570.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2pfu.ent.gz | 498.7 KB | Display | PDB format |
PDBx/mmJSON format | 2pfu.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/pf/2pfu ftp://data.pdbj.org/pub/pdb/validation_reports/pf/2pfu | 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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NMR ensembles |
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-Components
#1: Protein | Mass: 10906.492 Da / Num. of mol.: 1 / Fragment: Periplasmic domain (residues 44-141) / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / Strain: K12 / References: UniProt: P0ABV2 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample conditions | pH: 3 / Pressure: 1 atm / Temperature: 298 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||
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Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 20 / Conformers submitted total number: 19 |