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Open data
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Basic information
Entry | Database: PDB / ID: 9bl7 | ||||||||||||||||||||||||||||||
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Title | Mycobacterium tuberculosis efpA parallel dimer | ||||||||||||||||||||||||||||||
![]() | Uncharacterized MFS-type transporter EfpA | ||||||||||||||||||||||||||||||
![]() | MEMBRANE PROTEIN / Transporter | ||||||||||||||||||||||||||||||
Function / homology | ![]() | ||||||||||||||||||||||||||||||
Biological species | ![]() | ||||||||||||||||||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.22 Å | ||||||||||||||||||||||||||||||
![]() | Khandelwal, N.K. / Gupta, M. / Stroud, R.M. | ||||||||||||||||||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Mycobacterium tuberculosis EFPA parallel dimer Authors: Khandelwal, N.K. / Gupta, M. / Stroud, R.M. | ||||||||||||||||||||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 191.3 KB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 44651MC M: map data used to model this data C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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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: 66602.242 Da / Num. of mol.: 2 / Mutation: P171R Source method: isolated from a genetically manipulated source Details: Its a fusion protein where N terminal 48 residues of EfpA protein have been replaced by BRIL sequence. It contains P171R mutation in EfpA. Source: (gene. exp.) ![]() Gene: efpA, Rv2846c / Plasmid: pET28 / Production host: ![]() ![]() #2: Chemical | ChemComp-A1ATG / ( Mass: 736.912 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C40H65O10P Has ligand of interest | Y | 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
Component | Name: efflux protein A / Type: COMPLEX Details: Amino acid 1-4 start codon and GSSG 'expression tag', Amnio acid 5- 12 Flag tag, Amnio acid 13-15 SGS 'expression tag', Amino acid 16-21 thrombin site, Amino acid 22-128 BRIL-Tag, Amino acid ...Details: Amino acid 1-4 start codon and GSSG 'expression tag', Amnio acid 5- 12 Flag tag, Amnio acid 13-15 SGS 'expression tag', Amino acid 16-21 thrombin site, Amino acid 22-128 BRIL-Tag, Amino acid 129-610 Mycobacterium tuberculosis EfpA (truncated from 48 N terminal amino acid) with mutation of Proline at position 171 to Arginine, Amino acid 611-612 SS 'expression tag', Amino acid 613-619 TEV site, Amino acid 620-629 10XHis, Entity ID: #1 / Source: RECOMBINANT |
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Molecular weight | Value: 0.06653956 MDa / Experimental value: NO |
Source (natural) | Organism: ![]() |
Source (recombinant) | Organism: ![]() ![]() |
Buffer solution | pH: 7.5 / Details: 50mM Tris-HCL, 300 mM NaCL, 0.02% GDN, |
Specimen | Conc.: 16.16 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Specimen support | Details: 30 second hold 30 second glow / Grid material: GOLD / Grid mesh size: 400 divisions/in. / Grid type: Quantifoil R1.2/1.3 |
Vitrification | Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 281.15 K |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: OTHER / Nominal defocus max: 2000 nm / Nominal defocus min: 1000 nm / Cs: 2.7 mm / C2 aperture diameter: 70 µm |
Image recording | Electron dose: 45 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
EM software |
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CTF correction | Type: NONE | ||||||||||||
Particle selection | Num. of particles selected: 10225285 | ||||||||||||
Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||
3D reconstruction | Resolution: 3.22 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 174650 / Symmetry type: POINT |