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Title | Molecular interactions in rotavirus assembly and uncoating seen by high-resolution cryo-EM. |
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Journal, issue, pages | Proc Natl Acad Sci U S A, Vol. 106, Issue 26, Page 10644-10648, Year 2009 |
Publish date | Jun 30, 2009 |
Authors | James Z Chen / Ethan C Settembre / Scott T Aoki / Xing Zhang / A Richard Bellamy / Philip R Dormitzer / Stephen C Harrison / Nikolaus Grigorieff / |
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 ...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. |
External links | Proc Natl Acad Sci U S A / PubMed:19487668 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.8 - 5.5 Å |
Structure data | |
Chemicals | ChemComp-CA: ChemComp-ZN: |
Source |
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Keywords | VIRUS / rotavirus / VP7 / VP6 / VP2 / 7RP / DLP / Icosahedral virus / Capsid protein / Disulfide bond / Endoplasmic reticulum / Glycoprotein / Membrane / Transmembrane / Virion / Metal-binding / Zinc / Core protein / RNA-binding / Icosaderal virus |