6YGI

Duck hepatitis B virus capsid Mutant R124E_delta78-122

6YGI の概要

• エントリーDOI: 10.2210/pdb6ygi/pdb
• EMDBエントリー: 10800 10802 10803
• 分子名称: Capsid protein,Capsid protein (1 entity in total)
• 機能のキーワード: duck hepatitis b core protein, extension domain, spike, slowly folding, virus like particle
• 由来する生物種: Hepatitis B virus duck/DHBV-16 (DHBV); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 152975.93

構造登録者

Makbul, C.,Bottcher, B. (登録日: 2020-03-27, 公開日: 2020-09-02, 最終更新日: 2024-05-22)

主引用文献

Makbul, C.,Nassal, M.,Bottcher, B.
Slowly folding surface extension in the prototypic avian hepatitis B virus capsid governs stability.
Elife, 9:-, 2020

PubMed Abstract: Hepatitis B virus (HBV) is an important but difficult to study human pathogen. Most basics of the hepadnaviral life-cycle were unraveled using duck HBV (DHBV) as a model although DHBV has a capsid protein (CP) comprising ~260 rather than ~180 amino acids. Here we present high-resolution structures of several DHBV capsid-like particles (CLPs) determined by electron cryo-microscopy. As for HBV, DHBV CLPs consist of a dimeric α-helical frame-work with protruding spikes at the dimer interface. A fundamental new feature is a ~ 45 amino acid proline-rich extension in each monomer replacing the tip of the spikes in HBV CP. In vitro, folding of the extension takes months, implying a catalyzed process in vivo. DHBc variants lacking a folding-proficient extension produced regular CLPs in bacteria but failed to form stable nucleocapsids in hepatoma cells. We propose that the extension domain acts as a conformational switch with differential response options during viral infection.

PubMed: 32795390
DOI: 10.7554/eLife.57277

実験手法

ELECTRON MICROSCOPY (3 Å)