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5KHF

Fitted structure of rubella virus capsid protein

Summary for 5KHF
Entry DOI10.2210/pdb5khf/pdb
Related5KHC 5KHE
EMDB information8248 8249 8250 8251
Descriptorcapsid protein (2 entities in total)
Functional Keywordsrubella virus capsid protein, viral protein
Biological sourceRubella virus (RUBV)
Cellular locationCapsid protein: Virion . E1 envelope glycoprotein: Virion membrane ; Single-pass type I membrane protein . E2 envelope glycoprotein: Virion membrane ; Single-pass type I membrane protein : P07566
Total number of polymer chains2
Total formula weight60032.66
Authors
Mangala Prasad, V.,Klose, T.,Rossmann, M.G. (deposition date: 2016-06-14, release date: 2017-05-10, Last modification date: 2024-10-23)
Primary citationMangala Prasad, V.,Klose, T.,Rossmann, M.G.
Assembly, maturation and three-dimensional helical structure of the teratogenic rubella virus.
PLoS Pathog., 13:e1006377-e1006377, 2017
Cited by
PubMed Abstract: Viral infections during pregnancy are a significant cause of infant morbidity and mortality. Of these, rubella virus infection is a well-substantiated example that leads to miscarriages or severe fetal defects. However, structural information about the rubella virus has been lacking due to the pleomorphic nature of the virions. Here we report a helical structure of rubella virions using cryo-electron tomography. Sub-tomogram averaging of the surface spikes established the relative positions of the viral glycoproteins, which differed from the earlier icosahedral models of the virus. Tomographic analyses of in vitro assembled nucleocapsids and virions provide a template for viral assembly. Comparisons of immature and mature virions show large rearrangements in the glycoproteins that may be essential for forming the infectious virions. These results present the first known example of a helical membrane-enveloped virus, while also providing a structural basis for its assembly and maturation pathway.
PubMed: 28575072
DOI: 10.1371/journal.ppat.1006377
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (35 Å)
Structure validation

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数据于2025-06-25公开中

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