+Open data
-Basic information
Entry | Database: PDB / ID: 8xj8 | ||||||
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Title | The Cryo-EM structure of MPXV E5 C-terminal in complex with DNA | ||||||
Components |
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Keywords | REPLICATION / helicase | ||||||
Function / homology | Function and homology information helicase activity / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / host cell cytoplasm / hydrolase activity / ATP binding Similarity search - Function | ||||||
Biological species | Monkeypox virus | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.67 Å | ||||||
Authors | Zhang, W. / Liu, Y. / Gao, H. / Gan, J. | ||||||
Funding support | China, 1items
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Citation | Journal: Cell Discov / Year: 2024 Title: Structural and functional insights into the helicase protein E5 of Mpox virus. Authors: Gan, J. / Zhang, W. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8xj8.cif.gz | 404.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb8xj8.ent.gz | 323.3 KB | Display | PDB format |
PDBx/mmJSON format | 8xj8.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xj/8xj8 ftp://data.pdbj.org/pub/pdb/validation_reports/xj/8xj8 | HTTPS FTP |
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-Related structure data
Related structure data | 38396MC 8xifC 8xigC 8xj6C 8xj7C 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: DNA chain | Mass: 21440.668 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Monkeypox virus | ||||||
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#2: Protein | Mass: 53282.012 Da / Num. of mol.: 6 / Fragment: C-terminal Source method: isolated from a genetically manipulated source Source: (gene. exp.) Monkeypox virus / Gene: OPG117, MPXVgp100 / Production host: Escherichia coli (E. coli) References: UniProt: A0A7H0DN89, Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement #3: Chemical | #4: Chemical | 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: Monkeypox virus / Type: VIRUS / Entity ID: #1-#2 / Source: RECOMBINANT |
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Source (natural) | Organism: Monkeypox virus |
Source (recombinant) | Organism: Escherichia coli (E. coli) |
Details of virus | Empty: YES / Enveloped: YES / Isolate: SPECIES / Type: VIRION |
Buffer solution | pH: 8 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
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: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 2000 nm / Nominal defocus min: 1000 nm |
Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
-Processing
EM software | Name: PHENIX / Version: 1.19.1_4122: / Category: model refinement | ||||||||||||||||||||||||
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CTF correction | Type: NONE | ||||||||||||||||||||||||
3D reconstruction | Resolution: 2.67 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 247898 / Symmetry type: POINT | ||||||||||||||||||||||||
Refine LS restraints |
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