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Yorodumi- PDB-8uoy: Major interface of Streptococcal surface enolase dimer from AP53 ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 8uoy | ||||||
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Title | Major interface of Streptococcal surface enolase dimer from AP53 group A streptococcus bound to a lipid vesicle | ||||||
Components | Enolase | ||||||
Keywords | LYASE / Glycolysis / plasminogen binder / membrane protein | ||||||
Function / homology | Function and homology information phosphopyruvate hydratase / phosphopyruvate hydratase complex / phosphopyruvate hydratase activity / peptidoglycan-based cell wall / glycolytic process / cell surface / magnesium ion binding / extracellular region Similarity search - Function | ||||||
Biological species | Streptococcus pyogenes (bacteria) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.4 Å | ||||||
Authors | Tjia-Fleck, S. / Readnour, B.M. / Castellino, F.J. | ||||||
Funding support | United States, 1items
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Citation | Journal: To Be Published Title: Streptococcus surface alpha enolase exposed dimers were found to be the active form on lipid surface that binds to human plasminogen Authors: Tjia-Fleck, S. / Readnour, B.M. / Castellino, F.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8uoy.cif.gz | 277.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb8uoy.ent.gz | 227.8 KB | Display | PDB format |
PDBx/mmJSON format | 8uoy.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 8uoy_validation.pdf.gz | 1.1 MB | Display | wwPDB validaton report |
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Full document | 8uoy_full_validation.pdf.gz | 1.1 MB | Display | |
Data in XML | 8uoy_validation.xml.gz | 36.2 KB | Display | |
Data in CIF | 8uoy_validation.cif.gz | 53.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/uo/8uoy ftp://data.pdbj.org/pub/pdb/validation_reports/uo/8uoy | HTTPS FTP |
-Related structure data
Related structure data | 42441MC 8uopC 8uq6C C: citing same article (ref.) M: map data used to model this data |
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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: 47543.281 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Streptococcus pyogenes (bacteria) Gene: eno, E0F66_01300, E0F67_02490, FGO82_08975, SAMEA1711581_01820, SAMEA864267_00487 Production host: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria) References: UniProt: A3F8V6, phosphopyruvate hydratase |
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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: Streptococcal surface enolase major interface embedded into the surface of a lipid vesicle Type: COMPLEX / Entity ID: all / Source: RECOMBINANT |
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Molecular weight | Value: 0.095 MDa / Experimental value: YES |
Source (natural) | Organism: Streptococcus pyogenes (bacteria) |
Source (recombinant) | Organism: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria) |
Buffer solution | pH: 7.4 |
Specimen | 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: 298 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: SPOT SCAN |
Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 81000 X / Nominal defocus max: 29000 nm / Nominal defocus min: 1000 nm / Cs: 2.7 mm / Alignment procedure: BASIC |
Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Image recording | Electron dose: 60 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
-Processing
EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||
Particle selection | Num. of particles selected: 3300000 | ||||||||||||||||||
Symmetry | Point symmetry: C2 (2 fold cyclic) | ||||||||||||||||||
3D reconstruction | Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 476281 / Symmetry type: POINT |