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Yorodumi- EMDB-66330: focused map for HSV-1 helicase-primase in complex with ssDNA, ADP... -
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Basic information
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| Title | focused map for HSV-1 helicase-primase in complex with ssDNA, ADP and magnesium | |||||||||
Map data | focused map | |||||||||
Sample |
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Keywords | herpes simplex virus type 1 / helicase / primase / UL5 / UL52 / UL8 / DNA replication / Helicase superfamily I / SF1 / VIRAL PROTEIN / DNA BINDING PROTEIN | |||||||||
| Biological species | ![]() HSV-1 (Herpes simplex virus type 1) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.34 Å | |||||||||
Authors | Wu YQ / Jiang ZY / Chen XL / Zheng ZY / Dong CJ | |||||||||
| Funding support | China, 1 items
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Citation | Journal: Cell Discov / Year: 2025Title: Structural and mechanistic insights into the herpes simplex virus type 1 helicase-primase primosome. Authors: Yaqi Wu / Ziyi Jiang / Xiaoling Chen / Danyang Li / Zhengyu Zhang / Changjiang Dong / ![]() Abstract: DNA unwinding and primer synthesis are fundamental processes in genome replication. The human herpes simplex virus type 1 (HSV-1) helicase-primase forms a unique heterotrimeric primosome that is ...DNA unwinding and primer synthesis are fundamental processes in genome replication. The human herpes simplex virus type 1 (HSV-1) helicase-primase forms a unique heterotrimeric primosome that is essential for viral DNA unwinding and primer synthesis and represents an ideal drug target. However, its molecular mechanism remains poorly understood. Here we report the cryo-electron microscopic structure of the primosome in complex with single-stranded DNA, ADP and Mg to 3.47 Å resolution, which reveals that the primosome forms an unprecedented architecture in a fully open DNA binding groove between the helicase domains 1A and 2A-2B and that the primase subunit UL52 interacts extensively with the helicase subunit UL5 and accessory protein subunit UL8. Integrating mutagenesis, biochemical assays, structural analysis and 3D variability display analysis, we have identified the active sites of the ATPase, helicase and primase and critical interfaces between UL52, UL5 and UL8. Our work suggests that the primosome unwinds and translocates DNA via bidirectional rotation, and proposes a mechanistic model for DNA-dependent ATPase activation and alternating activity between helicase and primase. Herpesviridae family viruses pose significant threats to human health worldwide, and this trimeric assembly of primosomes is conserved. Our work provides a framework for understanding replication mechanisms across related viruses and for the rational design of broad-spectrum antivirals. | |||||||||
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_66330.map.gz | 398.7 MB | EMDB map data format | |
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| Header (meta data) | emd-66330-v30.xml emd-66330.xml | 13.7 KB 13.7 KB | Display Display | EMDB header |
| Images | emd_66330.png | 35 KB | ||
| Masks | emd_66330_msk_1.map | 421.9 MB | Mask map | |
| Filedesc metadata | emd-66330.cif.gz | 4.1 KB | ||
| Others | emd_66330_half_map_1.map.gz emd_66330_half_map_2.map.gz | 391.3 MB 391.2 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-66330 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-66330 | HTTPS FTP |
-Validation report
| Summary document | emd_66330_validation.pdf.gz | 1.2 MB | Display | EMDB validaton report |
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| Full document | emd_66330_full_validation.pdf.gz | 1.2 MB | Display | |
| Data in XML | emd_66330_validation.xml.gz | 17.9 KB | Display | |
| Data in CIF | emd_66330_validation.cif.gz | 21.2 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-66330 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-66330 | HTTPS FTP |
-Related structure data
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_66330.map.gz / Format: CCP4 / Size: 421.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | focused map | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.84 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Mask #1
| File | emd_66330_msk_1.map | ||||||||||||
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| Density Histograms |
-Half map: half map B for focused map
| File | emd_66330_half_map_1.map | ||||||||||||
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| Annotation | half map B for focused map | ||||||||||||
| Projections & Slices |
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| Density Histograms |
-Half map: half map A for focused map
| File | emd_66330_half_map_2.map | ||||||||||||
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| Annotation | half map A for focused map | ||||||||||||
| Projections & Slices |
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| Density Histograms |
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Sample components
-Entire : HSV-1 helicase-primase in complex with ssDNA, ADP and magnesium
| Entire | Name: HSV-1 helicase-primase in complex with ssDNA, ADP and magnesium |
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| Components |
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-Supramolecule #1: HSV-1 helicase-primase in complex with ssDNA, ADP and magnesium
| Supramolecule | Name: HSV-1 helicase-primase in complex with ssDNA, ADP and magnesium type: complex / ID: 1 / Parent: 0 |
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| Source (natural) | Organism: ![]() HSV-1 (Herpes simplex virus type 1) |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 7.5 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 50.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 0.8 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi



Keywords
HSV-1 (Herpes simplex virus type 1)
Authors
China, 1 items
Citation


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Processing
FIELD EMISSION GUN
