2YEW

Modeling Barmah Forest virus structural proteins

Summary for 2YEW

• Entry DOI: 10.2210/pdb2yew/pdb
• EMDB information: 1886
• Descriptor: CAPSID PROTEIN, E1 ENVELOPE GLYCOPROTEIN, E2 ENVELOPE GLYCOPROTEIN (3 entities in total)
• Functional Keywords: alphavirus, virus, molecular dynamics
• Biological source: BARMAH FOREST VIRUS; More
• Total number of polymer chains: 12
• Total formula weight: 483120.00

Authors

Kostyuchenko, V.A.,Jakana, J.,Liu, X.,Haddow, A.D.,Aung, M.,Weaver, S.C.,Chiu, W.,Lok, S.M. (deposition date: 2011-03-31, release date: 2012-04-18, Last modification date: 2024-10-23)

Primary citation

Kostyuchenko, V.A.,Jakana, J.,Liu, X.,Haddow, A.D.,Aung, M.,Weaver, S.C.,Chiu, W.,Lok, S.
The Structure of Barmah Forest Virus as Revealed by Cryo-Electron Microscopy at a 6-Angstrom Resolution Has Detailed Transmembrane Protein Architecture and Interactions.
J.Virol., 85:9327-, 2011

PubMed Abstract: Barmah Forest virus (BFV) is a mosquito-borne alphavirus that infects humans. A 6-Å-resolution cryo-electron microscopy three-dimensional structure of BFV exhibits a typical alphavirus organization, with RNA-containing nucleocapsid surrounded by a bilipid membrane anchored with the surface proteins E1 and E2. The map allows details of the transmembrane regions of E1 and E2 to be seen. The C-terminal end of the E2 transmembrane helix binds to the capsid protein. Following the E2 transmembrane helix, a short α-helical endodomain lies on the inner surface of the lipid envelope. The E2 endodomain interacts with E1 transmembrane helix from a neighboring E1-E2 trimeric spike, thereby acting as a spacer and a linker between spikes. In agreement with previous mutagenesis studies, the endodomain plays an important role in recruiting other E1-E2 spikes to the budding site during virus assembly. The E2 endodomain may thus serve as a target for antiviral drug design.

PubMed: 21752915
DOI: 10.1128/JVI.05015-11

Experimental method

ELECTRON MICROSCOPY (5 Å)