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Yorodumi- EMDB-17936: Structure of immature HTLV-1 CA-NTD from in vitro assembled MA126... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-17936 | |||||||||||||||
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Title | Structure of immature HTLV-1 CA-NTD from in vitro assembled MA126-CANC tubes: axis angle 10 degrees | |||||||||||||||
Map data | HTLV-1 MA126CANC tubes, axis angle 10, B-factor sharpened map | |||||||||||||||
Sample |
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Keywords | Retrovirus / HTLV / immature capsid / CA / CA-NTD / VIRAL PROTEIN | |||||||||||||||
Function / homology | Function and homology information | |||||||||||||||
Biological species | Human T-cell leukemia virus type I | |||||||||||||||
Method | subtomogram averaging / cryo EM / Resolution: 4.5 Å | |||||||||||||||
Authors | Obr M / Percipalle M / Chernikova D / Yang H / Thader A / Pinke G / Porley D / Mansky LM / Dick RA / Schur FKM | |||||||||||||||
Funding support | Austria, United States, 4 items
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Citation | Journal: Nat Struct Mol Biol / Year: 2024 Title: Distinct stabilization of the human T cell leukemia virus type 1 immature Gag lattice. Authors: Martin Obr / Mathias Percipalle / Darya Chernikova / Huixin Yang / Andreas Thader / Gergely Pinke / Dario Porley / Louis M Mansky / Robert A Dick / Florian K M Schur / Abstract: Human T cell leukemia virus type 1 (HTLV-1) immature particles differ in morphology from other retroviruses, suggesting a distinct way of assembly. Here we report the results of cryo-electron ...Human T cell leukemia virus type 1 (HTLV-1) immature particles differ in morphology from other retroviruses, suggesting a distinct way of assembly. Here we report the results of cryo-electron tomography studies of HTLV-1 virus-like particles assembled in vitro, as well as derived from cells. This work shows that HTLV-1 uses a distinct mechanism of Gag-Gag interactions to form the immature viral lattice. Analysis of high-resolution structural information from immature capsid (CA) tubular arrays reveals that the primary stabilizing component in HTLV-1 is the N-terminal domain of CA. Mutagenesis analysis supports this observation. This distinguishes HTLV-1 from other retroviruses, in which the stabilization is provided primarily by the C-terminal domain of CA. These results provide structural details of the quaternary arrangement of Gag for an immature deltaretrovirus and this helps explain why HTLV-1 particles are morphologically distinct. | |||||||||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_17936.map.gz | 51.6 MB | EMDB map data format | |
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Header (meta data) | emd-17936-v30.xml emd-17936.xml | 26.5 KB 26.5 KB | Display Display | EMDB header |
Images | emd_17936.png | 166.3 KB | ||
Filedesc metadata | emd-17936.cif.gz | 6.6 KB | ||
Others | emd_17936_half_map_1.map.gz emd_17936_half_map_2.map.gz | 28.4 MB 28.4 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-17936 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-17936 | HTTPS FTP |
-Validation report
Summary document | emd_17936_validation.pdf.gz | 1.1 MB | Display | EMDB validaton report |
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Full document | emd_17936_full_validation.pdf.gz | 1.1 MB | Display | |
Data in XML | emd_17936_validation.xml.gz | 11.7 KB | Display | |
Data in CIF | emd_17936_validation.cif.gz | 13.7 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-17936 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-17936 | HTTPS FTP |
-Related structure data
Related structure data | 8pudMC 8pu6C 8pu7C 8pu8C 8pu9C 8puaC 8pubC 8pucC 8pueC 8pufC 8pugC 8puhC C: citing same article (ref.) M: atomic model generated by this map |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_17936.map.gz / Format: CCP4 / Size: 55.4 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Annotation | HTLV-1 MA126CANC tubes, axis angle 10, B-factor sharpened map | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.327 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: HTLV-1 MA126CANC tubes, axis angle 10, halfmap 2
File | emd_17936_half_map_1.map | ||||||||||||
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Annotation | HTLV-1 MA126CANC tubes, axis angle 10, halfmap 2 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: HTLV-1 MA126CANC tubes, axis angle 10, halfmap 1
File | emd_17936_half_map_2.map | ||||||||||||
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Annotation | HTLV-1 MA126CANC tubes, axis angle 10, halfmap 1 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Human T-cell leukemia virus type I
Entire | Name: Human T-cell leukemia virus type I |
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Components |
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-Supramolecule #1: Human T-cell leukemia virus type I
Supramolecule | Name: Human T-cell leukemia virus type I / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / NCBI-ID: 11908 / Sci species name: Human T-cell leukemia virus type I / Virus type: VIRUS-LIKE PARTICLE / Virus isolate: STRAIN / Virus enveloped: No / Virus empty: Yes |
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-Macromolecule #1: Gag protein (Fragment)
Macromolecule | Name: Gag protein (Fragment) / type: protein_or_peptide / ID: 1 / Number of copies: 3 / Enantiomer: LEVO |
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Source (natural) | Organism: Human T-cell leukemia virus type I |
Molecular weight | Theoretical: 13.969809 KDa |
Recombinant expression | Organism: Escherichia coli BL21(DE3) (bacteria) |
Sequence | String: PVMHPHGAPP NHRPWQMKDL QAIKQEVSQA APGSPQFMQT IRLAVQQFDP TAKDLQDLLQ YLCSSLVASL HHQQLDSLIS EAETRGITG YNPLAGPLRV QANNPQQQGL RREYQQLWLA AFAALP UniProtKB: Gag protein |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | subtomogram averaging |
Aggregation state | helical array |
-Sample preparation
Buffer | pH: 8 Component:
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Grid | Model: C-flat-2/2 / Material: COPPER / Mesh: 300 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 30 sec. | |||||||||||||||
Vitrification | Cryogen name: ETHANE / Chamber humidity: 95 % / Chamber temperature: 283 K / Instrument: LEICA EM GP / Details: Grids coated with 2nm continuous carbon layer. |
-Electron microscopy #1
Microscopy ID | 1 |
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Microscope | FEI TITAN KRIOS |
Specialist optics | Energy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV |
Image recording | Image recording ID: 1 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Digitization - Dimensions - Width: 5760 pixel / Digitization - Dimensions - Height: 4092 pixel / Average exposure time: 0.3675 sec. / Average electron dose: 3.5 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: 4.0 µm / Nominal defocus min: 1.0 µm / Nominal magnification: 80000 |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Electron microscopy #1~
Microscopy ID | 1 |
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Microscope | FEI TITAN KRIOS |
Specialist optics | Energy filter - Name: GIF Quantum LS / Energy filter - Slit width: 20 eV |
Image recording | Image recording ID: 2 / Film or detector model: GATAN K2 QUANTUM (4k x 4k) / Detector mode: COUNTING / Digitization - Dimensions - Width: 3708 pixel / Digitization - Dimensions - Height: 3838 pixel / Average exposure time: 1.05 sec. / Average electron dose: 3.5 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: 3.5 µm / Nominal defocus min: 1.5 µm / Nominal magnification: 105000 |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
+Image processing
-Atomic model buiding 1
Initial model | Chain - Residue range: 13-125 / Chain - Source name: Other / Chain - Initial model type: other Details: rigid body fit derived from refined model deposited in D_1292131146 |
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Refinement | Space: REAL / Protocol: RIGID BODY FIT |
Output model | PDB-8pud: |