+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: Weizhen Zhang / Yusong Liu / Mengquan Yang / Jie Yang / Zhiwei Shao / Yanqing Gao / Xinran Jiang / Ruixue Cui / Yixi Zhang / Xin Zhao / Qiyuan Shao / Chulei Cao / Huili Li / Linxi Li / Hehua ...Authors: Weizhen Zhang / Yusong Liu / Mengquan Yang / Jie Yang / Zhiwei Shao / Yanqing Gao / Xinran Jiang / Ruixue Cui / Yixi Zhang / Xin Zhao / Qiyuan Shao / Chulei Cao / Huili Li / Linxi Li / Hehua Liu / Haishan Gao / Jianhua Gan / Abstract: Mpox virus (MPXV) can cause mpox in humans. Due to its quick and wide spread in the past two years, mpox has turned into a significant public health concern. Helicase E5 is a multi-domain protein; ...Mpox virus (MPXV) can cause mpox in humans. Due to its quick and wide spread in the past two years, mpox has turned into a significant public health concern. Helicase E5 is a multi-domain protein; its primer synthesis and DNA unwinding activity are required for genome uncoating and DNA replication of MPXV. However, the in vitro DNA unwinding activity has never been demonstrated. Here, we report the structural and biochemical studies of MPXV E5, showing that the full-length protein adopts an auto-inhibited conformation. Truncation of the N-terminus can recover the in vitro unwinding activity of E5 towards the forked DNA. Further structural analysis reveals that MPXV E5 shares a conserved mechanism in DNA unwinding and primer synthesis with the homologous proteins. These findings not only advance our understanding on the function of MPXV E5, but also provide a solid basis for the development of anti-poxvirus drugs. | ||||||
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 | 405.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb8xj8.ent.gz | 323.4 KB | Display | PDB format |
PDBx/mmJSON format | 8xj8.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 8xj8_validation.pdf.gz | 1.5 MB | Display | wwPDB validaton report |
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Full document | 8xj8_full_validation.pdf.gz | 1.5 MB | Display | |
Data in XML | 8xj8_validation.xml.gz | 66.6 KB | Display | |
Data in CIF | 8xj8_validation.cif.gz | 97.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xj/8xj8 ftp://data.pdbj.org/pub/pdb/validation_reports/xj/8xj8 | HTTPS FTP |
-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 FIELD / 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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