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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | Microbacterium phage Oxtober96 | |||||||||
![]() | Sharpened map of ewald sphere corrected map. | |||||||||
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![]() | HK97-fold / T=7 / tailed bacteriophage / VIRUS | |||||||||
Function / homology | Phage capsid / Phage capsid family / Major capsid protein![]() | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.2 Å | |||||||||
![]() | Podgorski JM / White SJ | |||||||||
Funding support | 1 items
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![]() | ![]() Title: A structural dendrogram of the actinobacteriophage major capsid proteins provides important structural insights into the evolution of capsid stability. Authors: Jennifer M Podgorski / Krista Freeman / Sophia Gosselin / Alexis Huet / James F Conway / Mary Bird / John Grecco / Shreya Patel / Deborah Jacobs-Sera / Graham Hatfull / Johann Peter Gogarten ...Authors: Jennifer M Podgorski / Krista Freeman / Sophia Gosselin / Alexis Huet / James F Conway / Mary Bird / John Grecco / Shreya Patel / Deborah Jacobs-Sera / Graham Hatfull / Johann Peter Gogarten / Janne Ravantti / Simon J White / ![]() ![]() Abstract: Many double-stranded DNA viruses, including tailed bacteriophages (phages) and herpesviruses, use the HK97-fold in their major capsid protein to make the capsomers of the icosahedral viral capsid. ...Many double-stranded DNA viruses, including tailed bacteriophages (phages) and herpesviruses, use the HK97-fold in their major capsid protein to make the capsomers of the icosahedral viral capsid. After the genome packaging at near-crystalline densities, the capsid is subjected to a major expansion and stabilization step that allows it to withstand environmental stresses and internal high pressure. Several different mechanisms for stabilizing the capsid have been structurally characterized, but how these mechanisms have evolved is still not understood. Using cryo-EM structure determination of 10 capsids, structural comparisons, phylogenetic analyses, and Alphafold predictions, we have constructed a detailed structural dendrogram describing the evolution of capsid structural stability within the actinobacteriophages. We show that the actinobacteriophage major capsid proteins can be classified into 15 groups based upon their HK97-fold. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 1.7 GB | ![]() | |
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Header (meta data) | ![]() ![]() | 20.2 KB 20.2 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 27.9 KB | Display | ![]() |
Images | ![]() | 257.4 KB | ||
Masks | ![]() | 1.9 GB | ![]() | |
Filedesc metadata | ![]() | 5.7 KB | ||
Others | ![]() ![]() ![]() | 1.6 GB 1.6 GB 1.6 GB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8ecoMC ![]() 8e16C ![]() 8eb4C ![]() 8ec2C ![]() 8ec8C ![]() 8eciC ![]() 8ecjC ![]() 8eckC ![]() 8ecnC ![]() 8eduC C: citing same article ( M: atomic model generated by this map |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Annotation | Sharpened map of ewald sphere corrected map. | ||||||||||||||||||||
Voxel size | X=Y=Z: 1.02182 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
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Density Histograms |
-Additional map: Map after CTF Refinement.
File | emd_28021_additional_1.map | ||||||||||||
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Annotation | Map after CTF Refinement. | ||||||||||||
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-Half map: Half map of ewald sphere corrected map.
File | emd_28021_half_map_1.map | ||||||||||||
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Annotation | Half map of ewald sphere corrected map. | ||||||||||||
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Density Histograms |
-Half map: Half map of ewald sphere corrected map.
File | emd_28021_half_map_2.map | ||||||||||||
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Annotation | Half map of ewald sphere corrected map. | ||||||||||||
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Density Histograms |
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Sample components
-Entire : Microbacterium phage Oxtober96
Entire | Name: ![]() |
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Components |
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-Supramolecule #1: Microbacterium phage Oxtober96
Supramolecule | Name: Microbacterium phage Oxtober96 / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / NCBI-ID: 2713266 / Sci species name: Microbacterium phage Oxtober96 / Virus type: VIRION / Virus isolate: STRAIN / Virus enveloped: No / Virus empty: No |
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Host (natural) | Organism: ![]() |
Virus shell | Shell ID: 1 / Diameter: 680.0 Å / T number (triangulation number): 7 |
-Macromolecule #1: Major capsid protein
Macromolecule | Name: Major capsid protein / type: protein_or_peptide / ID: 1 / Number of copies: 7 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 33.089148 KDa |
Sequence | String: MADISRADAL ALLATQELDS IIKPETSGSA ALAAFRSIRM SAGTVSMPVL AALPTAGWVT DDTSGAATGT KPTSKVSWTG KNLVAEEIA VIVPVHENTI ADSRFDIWGE VRPLVSQEFG RVLDEAVFFG VNKPATWLDP ALVPGAIAAG NTIADGTGID L ADDINEAF ...String: MADISRADAL ALLATQELDS IIKPETSGSA ALAAFRSIRM SAGTVSMPVL AALPTAGWVT DDTSGAATGT KPTSKVSWTG KNLVAEEIA VIVPVHENTI ADSRFDIWGE VRPLVSQEFG RVLDEAVFFG VNKPATWLDP ALVPGAIAAG NTIADGTGID L ADDINEAF GFVEDDEFDV NVAFTGRFLR RRLRGLRDAD NAPIYLDGVR SDNRTAEIYG QDLMYVGNRS WDRDEAVLLA GD RSKVLLG IREDVQVKLL TEATIGGINL AEKDMVALRF KFRVAYSTAF STAGGEVTDY PFAVITPDVT P UniProtKB: Major capsid protein |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Concentration | 10 mg/mL | ||||||||||||
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Buffer | pH: 7.5 Component:
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Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 283 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Detector mode: COUNTING / Number real images: 10437 / Average electron dose: 30.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.0 µm |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
-Atomic model buiding 1
Details | Amino acid sequence built into the map for a single major capsid protein and refined with Phenix. Model then used for rest of asymmetric unit and refined with Phenix. Final step involved using Isolde. |
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Refinement | Protocol: AB INITIO MODEL |
Output model | ![]() PDB-8eco: |