4JNT

Crystal structure of the ectodomain of Bovine viral diarrhea virus 1 E2 envelope protein

Summary for 4JNT

• Entry DOI: 10.2210/pdb4jnt/pdb
• Descriptor: Envelope glycoprotein E2, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total)
• Functional Keywords: bvdv1, e2, viral envelope protein, e2 envelope protein, viral membrane fusion, viral surface membrane, viral protein
• Biological source: Bovine viral diarrhea virus 1 (BVDV)
• Cellular location: E(rns) glycoprotein: Host membrane; Peripheral membrane protein. Envelope glycoprotein E2: Host cell surface. Cysteine protease NS2: Host membrane; Multi- pass membrane protein (Potential): P19711
• Total number of polymer chains: 2
• Total formula weight: 80457.40

Authors

Li, Y.,Wang, J.,Modis, Y. (deposition date: 2013-03-15, release date: 2013-04-17, Last modification date: 2024-11-06)

Primary citation

Li, Y.,Wang, J.,Kanai, R.,Modis, Y.
Crystal structure of glycoprotein E2 from bovine viral diarrhea virus.
Proc.Natl.Acad.Sci.USA, 110:6805-6810, 2013

PubMed Abstract: Pestiviruses, including bovine viral diarrhea virus, are important animal pathogens and are closely related to hepatitis C virus, which remains a major global health threat. They have an outer lipid envelope bearing two glycoproteins, E1 and E2, required for cell entry. They deliver their genome into the host cell cytoplasm by fusion of their envelope with a cellular membrane. The crystal structure of bovine viral diarrhea virus E2 reveals a unique protein architecture consisting of two Ig-like domains followed by an elongated β-stranded domain with a new fold. E2 forms end-to-end homodimers with a conserved C-terminal motif rich in aromatic residues at the contact. A disulfide bond across the interface explains the acid resistance of pestiviruses and their requirement for a redox activation step to initiate fusion. From the structure of E2, we propose alternative possible membrane fusion mechanisms. We expect the pestivirus fusion apparatus to be conserved in hepatitis C virus.

PubMed: 23569276
DOI: 10.1073/pnas.1300524110

Experimental method

X-RAY DIFFRACTION (4.09 Å)