3MKO

Crystal Structure of the Lymphocytic Choriomeningitis Virus Membrane Fusion Glycoprotein GP2 in its Postfusion Conformation

Summary for 3MKO

• Entry DOI: 10.2210/pdb3mko/pdb
• Descriptor: Glycoprotein C, (4S)-2-METHYL-2,4-PENTANEDIOL, CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: trimeric coiled-coil, viral protein
• Biological source: Lymphocytic choriomeningitis virus
• Total number of polymer chains: 1
• Total formula weight: 16781.22

Authors

Igonet, S.,Vaney, M.C.,Rey, F.A. (deposition date: 2010-04-15, release date: 2011-04-20, Last modification date: 2024-10-30)

Primary citation

Igonet, S.,Vaney, M.C.,Vonhrein, C.,Bricogne, G.,Stura, E.A.,Hengartner, H.,Eschli, B.,Rey, F.A.
X-ray structure of the arenavirus glycoprotein GP2 in its postfusion hairpin conformation
Proc.Natl.Acad.Sci.USA, 108:19967-19972, 2011

PubMed Abstract: Arenaviruses are important agents of zoonotic disease worldwide. The virions expose a tripartite envelope glycoprotein complex at their surface, formed by the glycoprotein subunits GP1, GP2 and the stable signal peptide. This complex is responsible for binding to target cells and for the subsequent fusion of viral and host-cell membranes for entry. During this process, the acidic environment of the endosome triggers a fusogenic conformational change in the transmembrane GP2 subunit of the complex. We report here the crystal structure of the recombinant GP2 ectodomain of the lymphocytic choriomeningitis virus, the arenavirus type species, at 1.8-Å resolution. The structure shows the characteristic trimeric coiled coil present in class I viral fusion proteins, with a central stutter that allows a close structural alignment with most of the available structures of class I and III viral fusion proteins. The structure further shows a number of intrachain salt bridges stabilizing the postfusion hairpin conformation, one of which involves an aspartic acid that appears released from a critical interaction with the stable signal peptide upon low pH activation.

PubMed: 22123988
DOI: 10.1073/pnas.1108910108

Experimental method

X-RAY DIFFRACTION (1.8 Å)