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-Structure paper
Title | Structural organization of pregenomic RNA and the carboxy-terminal domain of the capsid protein of hepatitis B virus. |
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Journal, issue, pages | PLoS Pathog, Vol. 8, Issue 9, Page e1002919, Year 2012 |
Publish date | Sep 20, 2012 |
Authors | Joseph C-Y Wang / Mary S Dhason / Adam Zlotnick / |
PubMed Abstract | The Hepatitis B Virus (HBV) double-stranded DNA genome is reverse transcribed from its RNA pregenome (pgRNA) within the virus core (or capsid). Phosphorylation of the arginine-rich carboxy-terminal ...The Hepatitis B Virus (HBV) double-stranded DNA genome is reverse transcribed from its RNA pregenome (pgRNA) within the virus core (or capsid). Phosphorylation of the arginine-rich carboxy-terminal domain (CTD) of the HBV capsid protein (Cp183) is essential for pgRNA encapsidation and reverse transcription. However, the structure of the CTD remains poorly defined. Here we report sub-nanometer resolution cryo-EM structures of in vitro assembled empty and pgRNA-filled Cp183 capsids in unphosphorylated and phosphorylation-mimic states. In empty capsids, we found unexpected evidence of surface accessible CTD density partially occluding pores in the capsid surface. We also observed that CTD organization changed substantively as a function of phosphorylation. In RNA-filled capsids, unphosphorylated CTDs favored thick ropes of RNA, while the phosphorylation-mimic favored a mesh of thin, high-density strands suggestive of single stranded RNA. These results demonstrate that the CTD can regulate nucleic acid structure, supporting the hypothesis that the HBV capsid has a functional role as a nucleic acid chaperone. |
External links | PLoS Pathog / PubMed:23028319 / PubMed Central |
Methods | EM (single particle) |
Resolution | 5.5 - 8.0 Å |
Structure data | EMDB-2057: EMDB-2058: EMDB-2059: EMDB-2060: |