+Open data
-Basic information
Entry | Database: PDB / ID: 8tss | ||||||||||||||||||
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Title | Open, inward-facing MsbA structure (OIF3) | ||||||||||||||||||
Components | ATP-binding transport protein MsbA | ||||||||||||||||||
Keywords | TRANSPORT PROTEIN / ABC transporter | ||||||||||||||||||
Function / homology | Function and homology information Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to catalyse transmembrane movement of substances / ATPase-coupled lipid transmembrane transporter activity / ABC-type transporter activity / ATP hydrolysis activity / ATP binding / plasma membrane Similarity search - Function | ||||||||||||||||||
Biological species | Escherichia coli (E. coli) | ||||||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.7 Å | ||||||||||||||||||
Authors | Yang, B. / Zhang, T. / Lyu, J. / Laganowsky, A.D. / Zhao, M. | ||||||||||||||||||
Funding support | United States, 5items
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Citation | Journal: To Be Published Title: Native mass spectrometry captures snapshots of the MsbA transport cycle Authors: Zhang, T. / Lyu, J. / Yang, B. / Zhao, M. / Laganowsky, A.D. | ||||||||||||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8tss.cif.gz | 199.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb8tss.ent.gz | 161.5 KB | Display | PDB format |
PDBx/mmJSON format | 8tss.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 8tss_validation.pdf.gz | 1.2 MB | Display | wwPDB validaton report |
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Full document | 8tss_full_validation.pdf.gz | 1.2 MB | Display | |
Data in XML | 8tss_validation.xml.gz | 45.5 KB | Display | |
Data in CIF | 8tss_validation.cif.gz | 67.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ts/8tss ftp://data.pdbj.org/pub/pdb/validation_reports/ts/8tss | HTTPS FTP |
-Related structure data
Related structure data | 41600MC 8tsoC 8tspC 8tsqC 8tsrC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
#1: Protein | Mass: 64543.473 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Production host: Escherichia coli (E. coli) References: UniProt: C3TGA2, Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to catalyse transmembrane movement of substances |
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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 |
-Sample preparation
Component | Name: E. coli MsbA incubated with ATP for 6 hours / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT |
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Source (natural) | Organism: Escherichia coli (E. coli) |
Source (recombinant) | Organism: Escherichia coli (E. coli) |
Buffer solution | pH: 7.4 |
Specimen | Conc.: 8 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 281 K |
-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: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2500 nm / Nominal defocus min: 1000 nm |
Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
-Processing
EM software |
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CTF correction | Type: PHASE FLIPPING ONLY | ||||||||||||||||||||||||
3D reconstruction | Resolution: 3.7 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 91092 / Symmetry type: POINT | ||||||||||||||||||||||||
Atomic model building | Protocol: AB INITIO MODEL / Space: REAL | ||||||||||||||||||||||||
Refine LS restraints |
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