7TUK
Small hepatitis B virus surface protein without cytosolic and antigenic loops
Summary for 7TUK
| Entry DOI | 10.2210/pdb7tuk/pdb |
| EMDB information | 26117 |
| Descriptor | SAg protein (1 entity in total) |
| Functional Keywords | hbv, svp, hbsag, envelope protein, viral protein |
| Biological source | HBV genotype E |
| Total number of polymer chains | 2 |
| Total formula weight | 50607.98 |
| Authors | Liu, H.,Wang, J.C.Y. (deposition date: 2022-02-02, release date: 2022-08-24, Last modification date: 2024-02-21) |
| Primary citation | Liu, H.,Hong, X.,Xi, J.,Menne, S.,Hu, J.,Wang, J.C. Cryo-EM structures of human hepatitis B and woodchuck hepatitis virus small spherical subviral particles. Sci Adv, 8:eabo4184-eabo4184, 2022 Cited by PubMed Abstract: The loss of detectable hepatitis B surface antigen (HBsAg) is considered a functional cure in chronic hepatitis B. Naturally, HBsAg can be incorporated into the virion envelope or assembled into subviral particles (SVPs) with lipid from host cells. Until now, there has been no detailed structure of HBsAg, and the published SVP structures are controversial. Here, we report the first subnanometer-resolution structures of spherical SVP from hepatitis B virus (HBV) and the related woodchuck hepatitis virus (WHV) determined by cryo-electron microscopy in combination with AlphaFold2 prediction. Both structures showed unique rhombicuboctahedral symmetry with 24 protruding spikes comprising dimer of small HBsAg with four helical domains. The lipid moiety in the SVP is organized in a noncanonical lipid patch instead of a lipid bilayer, which can accommodate the exposed hydrophobic surface and modulate particle stability. Together, these findings advance our knowledge of viral membrane organization and the structures of HBV and WHV spherical SVPs. PubMed: 35930632DOI: 10.1126/sciadv.abo4184 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (6.3 Å) |
Structure validation
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