3GZU

VP7 recoated rotavirus DLP

Summary for 3GZU

• Entry DOI: 10.2210/pdb3gzu/pdb
• Related: 3GZT
• EMDB information: 1571 1609
• Descriptor: Inner capsid protein VP2, Intermediate capsid protein VP6, ZINC ION (3 entities in total)
• Functional Keywords: rotavirus, vp7, vp6, vp2, 7rp, dlp, capsid protein, metal-binding, virion, zinc, core protein, rna-binding, icosaderal virus, virus
• Biological source: Rotavirus A (RV-A); More
• Total number of polymer chains: 15
• Total formula weight: 770017.25

Authors

Chen, J.Z.,Settembre, E.C.,Harrison, S.C.,Grigorieff, N. (deposition date: 2009-04-07, release date: 2009-07-14, Last modification date: 2024-02-21)

Primary citation

Chen, J.Z.,Settembre, E.C.,Aoki, S.T.,Zhang, X.,Bellamy, A.R.,Dormitzer, P.R.,Harrison, S.C.,Grigorieff, N.
Molecular interactions in rotavirus assembly and uncoating seen by high-resolution cryo-EM.
Proc.Natl.Acad.Sci.USA, 106:10644-10648, 2009

PubMed Abstract: Rotaviruses, major causes of childhood gastroenteritis, are nonenveloped, icosahedral particles with double-strand RNA genomes. By the use of electron cryomicroscopy and single-particle reconstruction, we have visualized a rotavirus particle comprising the inner capsid coated with the trimeric outer-layer protein, VP7, at a resolution (4 A) comparable with that of X-ray crystallography. We have traced the VP7 polypeptide chain, including parts not seen in its X-ray crystal structure. The 3 well-ordered, 30-residue, N-terminal "arms" of each VP7 trimer grip the underlying trimer of VP6, an inner-capsid protein. Structural differences between free and particle-bound VP7 and between free and VP7-coated inner capsids may regulate mRNA transcription and release. The Ca(2+)-stabilized VP7 intratrimer contact region, which presents important neutralizing epitopes, is unaltered upon capsid binding.

PubMed: 19487668
DOI: 10.1073/pnas.0904024106

Experimental method

ELECTRON MICROSCOPY (3.8 Å)