3HAG

Crystal structure of the Hepatitis E Virus-like Particle

Summary for 3HAG

• Entry DOI: 10.2210/pdb3hag/pdb
• Descriptor: Capsid protein (1 entity in total)
• Functional Keywords: jelly-roll beta sheets, beta barrel, virus, icosahedral virus
• Biological source: Hepatitis E virus type 4
• Total number of polymer chains: 1
• Total formula weight: 54446.56

Authors

Guu, T.S.Y.,Liu, Z.,Ye, Q.,Mata, D.A.,Li, K.,Yin, C.,Zhang, J.,Tao, Y.J. (deposition date: 2009-05-01, release date: 2009-09-01, Last modification date: 2024-04-03)

Primary citation

Guu, T.S.,Liu, Z.,Ye, Q.,Mata, D.A.,Li, K.,Yin, C.,Zhang, J.,Tao, Y.J.
Structure of the hepatitis E virus-like particle suggests mechanisms for virus assembly and receptor binding.
Proc.Natl.Acad.Sci.USA, 106:12992-12997, 2009

PubMed Abstract: Hepatitis E virus (HEV), a small, non-enveloped RNA virus in the family Hepeviridae, is associated with endemic and epidemic acute viral hepatitis in developing countries. Our 3.5-A structure of a HEV-like particle (VLP) shows that each capsid protein contains 3 linear domains that form distinct structural elements: S, the continuous capsid; P1, 3-fold protrusions; and P2, 2-fold spikes. The S domain adopts a jelly-roll fold commonly observed in small RNA viruses. The P1 and P2 domains both adopt beta-barrel folds. Each domain possesses a potential polysaccharide-binding site that may function in cell-receptor binding. Sugar binding to P1 at the capsid protein interface may lead to capsid disassembly and cell entry. Structural modeling indicates that native T = 3 capsid contains flat dimers, with less curvature than those of T = 1 VLP. Our findings significantly advance the understanding of HEV molecular biology and have application to the development of vaccines and antiviral medications.

PubMed: 19622744
DOI: 10.1073/pnas.0904848106

Experimental method

X-RAY DIFFRACTION (3.5 Å)