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4HBO

Crystal Structure of Rubella virus capsid protein (residues 127-277)

Summary for 4HBO
Entry DOI10.2210/pdb4hbo/pdb
Related4HAR 4HBE
DescriptorCapsid protein (1 entity in total)
Functional Keywordspartial beta barrel, capsid protein, viral protein
Biological sourceRubella virus (RUBV)
Total number of polymer chains5
Total formula weight74937.01
Authors
Mangala Prasad, V.,Fokine, A.,Rossmann, M.G. (deposition date: 2012-09-28, release date: 2013-12-11, Last modification date: 2023-12-06)
Primary citationMangala Prasad, V.,Willows, S.D.,Fokine, A.,Battisti, A.J.,Sun, S.,Plevka, P.,Hobman, T.C.,Rossmann, M.G.
Rubella virus capsid protein structure and its role in virus assembly and infection.
Proc.Natl.Acad.Sci.USA, 110:20105-20110, 2013
Cited by
PubMed Abstract: Rubella virus (RV) is a leading cause of birth defects due to infectious agents. When contracted during pregnancy, RV infection leads to severe damage in fetuses. Despite its medical importance, compared with the related alphaviruses, very little is known about the structure of RV. The RV capsid protein is an essential structural component of virions as well as a key factor in virus-host interactions. Here we describe three crystal structures of the structural domain of the RV capsid protein. The polypeptide fold of the RV capsid protomer has not been observed previously. Combining the atomic structure of the RV capsid protein with the cryoelectron tomograms of RV particles established a low-resolution structure of the virion. Mutational studies based on this structure confirmed the role of amino acid residues in the capsid that function in the assembly of infectious virions.
PubMed: 24282305
DOI: 10.1073/pnas.1316681110
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.241 Å)
Structure validation

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