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Open data
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Basic information
| Entry | Database: PDB / ID: 9p52 | ||||||||||||
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| Title | LptBFGCA from Escherichia coli | ||||||||||||
Components |
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Keywords | LIPID TRANSPORT / Complex / Lipopolysaccharide / ABC / ATP binding cassette / transporter | ||||||||||||
| Function / homology | Function and homology informationlipopolysaccharide transfer activity / Translocases; Catalysing the translocation of carbohydrates and their derivatives; Linked to the hydrolysis of a nucleoside triphosphate / glycolipid transfer activity / transporter complex / lipopolysaccharide transport / Gram-negative-bacterium-type cell outer membrane assembly / ATP-binding cassette (ABC) transporter complex / cell outer membrane / lipopolysaccharide binding / transmembrane transport ...lipopolysaccharide transfer activity / Translocases; Catalysing the translocation of carbohydrates and their derivatives; Linked to the hydrolysis of a nucleoside triphosphate / glycolipid transfer activity / transporter complex / lipopolysaccharide transport / Gram-negative-bacterium-type cell outer membrane assembly / ATP-binding cassette (ABC) transporter complex / cell outer membrane / lipopolysaccharide binding / transmembrane transport / outer membrane-bounded periplasmic space / periplasmic space / ATP hydrolysis activity / ATP binding / membrane / identical protein binding / plasma membrane / cytoplasm Similarity search - Function | ||||||||||||
| Biological species | ![]() | ||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.1 Å | ||||||||||||
Authors | Taylor, R.J. / Pahil, K.S. / Walsh Jr., R.M. / Kahne, D.E. | ||||||||||||
| Funding support | United States, 3items
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Citation | Journal: To Be PublishedTitle: Structural basis for regulating lipopolysaccharide transmembrane transport Authors: Taylor, R.J. / Pahil, K.S. / Walsh Jr., R.M. / Kahne, D.E. | ||||||||||||
| History |
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 9p52.cif.gz | 393.5 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9p52.ent.gz | 319.7 KB | Display | PDB format |
| PDBx/mmJSON format | 9p52.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/p5/9p52 ftp://data.pdbj.org/pub/pdb/validation_reports/p5/9p52 | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 71298MC ![]() 9p7mC ![]() 9p7pC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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| 1 |
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Components
| #1: Protein | Mass: 26593.312 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: P0A9V1, Translocases; Catalysing the translocation of carbohydrates and their derivatives; Linked to the hydrolysis of a nucleoside triphosphate #2: Protein | | Mass: 42059.082 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: Expressed as a fusion with His-tagged LptA,Expressed as a fusion with His-tagged LptA Source: (gene. exp.) ![]() ![]() #3: Protein | | Mass: 40393.473 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #4: Protein | | Mass: 39651.410 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Has protein modification | N | |
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-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
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| Molecular weight | Experimental value: NO | |||||||||||||||||||||||||||||||||||
| Source (natural) |
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| Source (recombinant) |
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| Buffer solution | pH: 8 Details: 20mM Tris HCl, 150mM NaCl, 1% glycerol, 1% DMSO, 1% ethylene glycol, 0.02% GDN | |||||||||||||||||||||||||||||||||||
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| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES / Details: This sample was monodisperse as determined by SEC. | |||||||||||||||||||||||||||||||||||
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277 K |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2200 nm / Nominal defocus min: 1100 nm |
| Image recording | Electron dose: 58 e/Å2 / Film or detector model: GATAN K3 BIOCONTINUUM (6k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| Particle selection | Num. of particles selected: 3100000 | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 697837 / Symmetry type: POINT |
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FIELD EMISSION GUN