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Yorodumi- PDB-8jo4: Cryo-EM structure of a Legionella effector complexed with actin a... -
+Open data
-Basic information
Entry | Database: PDB / ID: 8jo4 | |||||||||||||||
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Title | Cryo-EM structure of a Legionella effector complexed with actin and ATP | |||||||||||||||
Components |
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Keywords | TOXIN / AMPylation | |||||||||||||||
Function / homology | Function and homology information cytoskeletal motor activator activity / tropomyosin binding / myosin heavy chain binding / mesenchyme migration / troponin I binding / actin filament bundle / filamentous actin / skeletal muscle thin filament assembly / actin filament bundle assembly / striated muscle thin filament ...cytoskeletal motor activator activity / tropomyosin binding / myosin heavy chain binding / mesenchyme migration / troponin I binding / actin filament bundle / filamentous actin / skeletal muscle thin filament assembly / actin filament bundle assembly / striated muscle thin filament / skeletal muscle myofibril / actin monomer binding / skeletal muscle fiber development / stress fiber / titin binding / actin filament polymerization / filopodium / actin filament / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / calcium-dependent protein binding / lamellipodium / cell body / hydrolase activity / protein domain specific binding / calcium ion binding / positive regulation of gene expression / magnesium ion binding / ATP binding / identical protein binding / cytoplasm Similarity search - Function | |||||||||||||||
Biological species | Legionella sainthelensi (bacteria) Oryctolagus cuniculus (rabbit) | |||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.04 Å | |||||||||||||||
Authors | Zhou, X.T. / Wang, X.F. / Tan, J.X. / Zhu, Y.Q. | |||||||||||||||
Funding support | China, 4items
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Citation | Journal: To Be Published Title: Cryo-EM structure of a Legionella effector complexed with actin and ATP Authors: Zhou, X.T. / Wang, X.F. / Tan, J.X. / Zhu, Y.Q. | |||||||||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8jo4.cif.gz | 155.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb8jo4.ent.gz | 118.3 KB | Display | PDB format |
PDBx/mmJSON format | 8jo4.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jo/8jo4 ftp://data.pdbj.org/pub/pdb/validation_reports/jo/8jo4 | HTTPS FTP |
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-Related structure data
Related structure data | 36455MC 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: 50352.203 Da / Num. of mol.: 1 / Mutation: H287A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Legionella sainthelensi (bacteria) / Gene: CAB17_03485 / Production host: Escherichia coli BL21 (bacteria) / References: UniProt: A0A2H5FI52 | ||||||
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#2: Protein | Mass: 42096.953 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Oryctolagus cuniculus (rabbit) References: UniProt: P68135, Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement | ||||||
#3: Chemical | #4: Chemical | ChemComp-MG / | #5: Chemical | ChemComp-CA / | Has ligand of interest | Y | |
-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: Cryo-EM structure of a Legionella effector complexed with actin and ATP Type: COMPLEX / Entity ID: #1-#2 / Source: MULTIPLE SOURCES |
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Molecular weight | Experimental value: NO |
Source (natural) | Organism: Legionella sainthelensi (bacteria) |
Source (recombinant) | Organism: Escherichia coli (E. coli) |
Buffer solution | pH: 8 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Specimen support | Grid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R0.6/1 |
Vitrification | Cryogen name: ETHANE |
-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 FIELDBright-field microscopy / Nominal defocus max: 1600 nm / Nominal defocus min: 800 nm |
Image recording | Electron dose: 50 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k) |
-Processing
EM software | Name: PHENIX / Version: dev_4694: / Category: model refinement | ||||||||||||||||||||||||
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||||||||||||||
3D reconstruction | Resolution: 3.04 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 171800 / Symmetry type: POINT | ||||||||||||||||||||||||
Atomic model building | Details: ModelAngelo built model / Source name: Other / Type: in silico model | ||||||||||||||||||||||||
Refine LS restraints |
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