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9CGM

The Structure of Spiroplasma Virus 4

This is a non-PDB format compatible entry.
Summary for 9CGM
Entry DOI10.2210/pdb9cgm/pdb
EMDB information45583
DescriptorCapsid protein VP1, DNA binding protein ORF8 (2 entities in total)
Functional Keywordsmicroviridae; bacteriophage; capsid; spiroplasma virus 4; spv4, virus
Biological sourceSpiromicrovirus SpV4
More
Total number of polymer chains120
Total formula weight4016331.78
Authors
Mietzsch, M.,McKenna, R. (deposition date: 2024-06-30, release date: 2024-07-17, Last modification date: 2024-08-07)
Primary citationMietzsch, 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: 39066266
DOI: 10.3390/v16071103
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.52 Å)
Structure validation

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