+検索条件
-Structure paper
タイトル | Structural organization of pregenomic RNA and the carboxy-terminal domain of the capsid protein of hepatitis B virus. |
---|---|
ジャーナル・号・ページ | PLoS Pathog, Vol. 8, Issue 9, Page e1002919, Year 2012 |
掲載日 | 2012年9月20日 |
著者 | Joseph C-Y Wang / Mary S Dhason / Adam Zlotnick / |
PubMed 要旨 | 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. |
リンク | PLoS Pathog / PubMed:23028319 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 5.5 - 8.0 Å |
構造データ | EMDB-2057: EMDB-2058: EMDB-2059: EMDB-2060: |