Summary for 9CGM
Entry DOI | 10.2210/pdb9cgm/pdb |
EMDB information | 45583 |
Descriptor | Capsid protein VP1, DNA binding protein ORF8 (2 entities in total) |
Functional Keywords | microviridae; bacteriophage; capsid; spiroplasma virus 4; spv4, virus |
Biological source | Spiromicrovirus SpV4 More |
Total number of polymer chains | 120 |
Total formula weight | 4016331.78 |
Authors | Mietzsch, M.,McKenna, R. (deposition date: 2024-06-30, release date: 2024-07-17, Last modification date: 2024-08-07) |
Primary citation | Mietzsch, M.,Kailasan, S.,Bennett, A.,Chipman, P.,Fane, B.,Huiskonen, J.T.,Clarke, I.N.,McKenna, R. The Structure of Spiroplasma Virus 4 : Exploring the Capsid Diversity of the Microviridae. Viruses, 16:-, 2024 Cited by PubMed Abstract: (SpV4) is a bacteriophage of the , which packages circular ssDNA within non-enveloped T = 1 icosahedral capsids. It infects spiroplasmas, which are known pathogens of honeybees. Here, the structure of the SpV4 virion is determined using cryo-electron microscopy to a resolution of 2.5 Å. A striking feature of the SpV4 capsid is the mushroom-like protrusions at the 3-fold axes, which is common among all members of the subfamily While the function of the protrusion is currently unknown, this feature varies widely in this subfamily and is therefore possibly an adaptation for host recognition. Furthermore, on the interior of the SpV4 capsid, the location of DNA-binding protein VP8 was identified and shown to have low structural conservation to the capsids of other viruses in the family. The structural characterization of SpV4 will aid future studies analyzing the virus-host interaction, to understand disease mechanisms at a molecular level. Furthermore, the structural comparisons in this study, including a low-resolution structure of the chlamydia phage 2, provide an overview of the structural repertoire of the viruses in this family that infect various bacterial hosts, which in turn infect a wide range of animals and plants. PubMed: 39066266DOI: 10.3390/v16071103 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (2.52 Å) |
Structure validation
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