6YGH
Duck hepatitis B virus capsid
Summary for 6YGH
| Entry DOI | 10.2210/pdb6ygh/pdb |
| EMDB information | 10800 |
| Descriptor | Capsid protein (1 entity in total) |
| Functional Keywords | duck hepatitis b core protein, extension domain, spike, slowly folding, virus like particle |
| Biological source | Hepatitis B virus duck/DHBV-16 (DHBV) |
| Total number of polymer chains | 6 |
| Total formula weight | 182031.06 |
| Authors | Makbul, C.,Bottcher, B. (deposition date: 2020-03-27, release date: 2020-09-02, Last modification date: 2024-05-22) |
| Primary citation | Makbul, C.,Nassal, M.,Bottcher, B. Slowly folding surface extension in the prototypic avian hepatitis B virus capsid governs stability. Elife, 9:-, 2020 Cited by 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: 32795390DOI: 10.7554/eLife.57277 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.7 Å) |
Structure validation
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