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Open data
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Basic information
| Entry | ![]() | ||||||||||||
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| Title | CAEV CA Hexamer Assembled via Liposome Templating | ||||||||||||
Map data | EM Map of CAEV CA Hexamer solved via liposome templating. | ||||||||||||
Sample | Caprine arthritis encephalitis virus strain Cork != Caprine arthritis encephalitis virus Caprine arthritis encephalitis virus strain Cork
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Keywords | CAEV / Capsid / Hexamer / Viral Protein | ||||||||||||
| Function / homology | Function and homology informationviral budding via host ESCRT complex / viral capsid / nucleic acid binding / zinc ion binding Similarity search - Function | ||||||||||||
| Biological species | Caprine arthritis encephalitis virus | ||||||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.0 Å | ||||||||||||
Authors | Arizaga F / Freniere C / Xiong Y | ||||||||||||
| Funding support | United States, 3 items
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Citation | Journal: J Am Chem Soc / Year: 2025Title: Exploring the Structural Divergence of HIV and SRLV Lentiviral Capsids. Authors: Fidel Arizaga / Christian Freniere / Juan S Rey / Matthew Cook / Chunxiang Wu / Juan R Perilla / Yong Xiong / ![]() Abstract: Lentiviruses require a mature capsid to package and traffic their viral genome for successful infection and propagation. Although the HIV-1 capsid structure has been extensively studied, structural ...Lentiviruses require a mature capsid to package and traffic their viral genome for successful infection and propagation. Although the HIV-1 capsid structure has been extensively studied, structural information is lacking for other lentiviral capsids, limiting our understanding. Using cryo-electron microscopy (cryo-EM) and a liposome-templating system, we assembled capsid-like particles (CLPs) and resolved capsid protein (CA) pentamer and hexamer lattice structures from the two major phylogenetic groups of small ruminant lentiviruses (SRLVs). These structures exhibit an overall lattice organization like HIV-1 but differ in key characteristics, notably the absence of inositol hexakisphosphate (IP6) in the SRLV CA lattice─a critical factor for HIV-1 capsid assembly and function. Additionally, SRLV CA pentamers show a unique N-terminal domain orientation, providing insights into SRLV capsid assembly mechanisms. These observations, together with our molecular dynamics (MD) simulation, results suggest a possible mechanism for importing deoxynucleotide triphosphate (dNTP) molecules into SRLV capsids. Furthermore, key regions of host factor interaction, such as the CypA binding motifs, have diverged in the SRLV CA assemblies. Our results contribute to understanding the SRLV lentiviral capsids which may facilitate structure-based inhibitor design strategies. | ||||||||||||
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_48335.map.gz | 112.8 MB | EMDB map data format | |
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| Header (meta data) | emd-48335-v30.xml emd-48335.xml | 17.2 KB 17.2 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_48335_fsc.xml | 13.3 KB | Display | FSC data file |
| Images | emd_48335.png | 114.3 KB | ||
| Masks | emd_48335_msk_1.map | 244.1 MB | Mask map | |
| Filedesc metadata | emd-48335.cif.gz | 5.8 KB | ||
| Others | emd_48335_half_map_1.map.gz emd_48335_half_map_2.map.gz | 226.1 MB 226.1 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-48335 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-48335 | HTTPS FTP |
-Validation report
| Summary document | emd_48335_validation.pdf.gz | 999.5 KB | Display | EMDB validaton report |
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| Full document | emd_48335_full_validation.pdf.gz | 999.1 KB | Display | |
| Data in XML | emd_48335_validation.xml.gz | 22.2 KB | Display | |
| Data in CIF | emd_48335_validation.cif.gz | 28.8 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-48335 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-48335 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9mkrMC ![]() 9mkpC ![]() 9mkqC ![]() 9mksC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_48335.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | EM Map of CAEV CA Hexamer solved via liposome templating. | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.53 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Mask #1
| File | emd_48335_msk_1.map | ||||||||||||
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| Density Histograms |
-Half map: EM Half Map A of CAEV CA Hexamer solved via liposome templating.
| File | emd_48335_half_map_1.map | ||||||||||||
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| Annotation | EM Half Map A of CAEV CA Hexamer solved via liposome templating. | ||||||||||||
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| Density Histograms |
-Half map: EM Half Map B of CAEV CA Hexamer solved via liposome templating.
| File | emd_48335_half_map_2.map | ||||||||||||
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| Annotation | EM Half Map B of CAEV CA Hexamer solved via liposome templating. | ||||||||||||
| Projections & Slices |
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| Density Histograms |
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Sample components
-Entire : Caprine arthritis encephalitis virus strain Cork
| Entire | Name: Caprine arthritis encephalitis virus strain Cork |
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| Components |
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-Supramolecule #1: Caprine arthritis encephalitis virus
| Supramolecule | Name: Caprine arthritis encephalitis virus / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / NCBI-ID: 11661 / Sci species name: Caprine arthritis encephalitis virus / Sci species strain: strain Cork / Virus type: VIRUS-LIKE PARTICLE / Virus isolate: STRAIN / Virus enveloped: No / Virus empty: Yes |
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| Host (natural) | Organism: ![]() |
-Macromolecule #1: Capsid protein p25
| Macromolecule | Name: Capsid protein p25 / type: protein_or_peptide / ID: 1 / Details: CAEV CA with C-terminal His tag. / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: Caprine arthritis encephalitis virus / Strain: Cork |
| Molecular weight | Theoretical: 25.625027 KDa |
| Recombinant expression | Organism: ![]() |
| Sequence | String: PIVVQAAGGR SWKAVDSVMF QQLQTVAMQH GLVSEDFERQ LAYYATTWTS KDILEVLAMM PGNRAQKELI QGKLNEEAER WRRNNPPPP AGGGLTVDQI MGVGQTNQAA AQANMDQARQ ICLQWVINAL RAVRHMAHRP GNPMLVKQKT NEPYEDFAAR L LEAIDAEP ...String: PIVVQAAGGR SWKAVDSVMF QQLQTVAMQH GLVSEDFERQ LAYYATTWTS KDILEVLAMM PGNRAQKELI QGKLNEEAER WRRNNPPPP AGGGLTVDQI MGVGQTNQAA AQANMDQARQ ICLQWVINAL RAVRHMAHRP GNPMLVKQKT NEPYEDFAAR L LEAIDAEP VTQPIKDYLK LTLSYTNASA DCQKQMDRTL GQRVQQASVE EKMQACRDVG SEGFHHHHHH UniProtKB: Gag polyprotein |
-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: 8 |
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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 / Cs: 2.7 mm / Nominal defocus max: 2.8000000000000003 µm / Nominal defocus min: 0.5 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
| Initial model | Chain - Source name: Other / Chain - Initial model type: in silico model / Details: ModelAngelo |
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| Output model | ![]() PDB-9mkr: |
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About Yorodumi




Caprine arthritis encephalitis virus
Keywords
Authors
United States, 3 items
Citation








Z (Sec.)
Y (Row.)
X (Col.)














































FIELD EMISSION GUN

