1EBO

CRYSTAL STRUCTURE OF THE EBOLA VIRUS MEMBRANE-FUSION SUBUNIT, GP2, FROM THE ENVELOPE GLYCOPROTEIN ECTODOMAIN

Summary for 1EBO

• Entry DOI: 10.2210/pdb1ebo/pdb
• Descriptor: EBOLA VIRUS ENVELOPE PROTEIN CHIMERA CONSISTING OF A FRAGMENT OF GCN4 ZIPPER CLONED N-TERMINAL TO A FRAGMENT OF GP2, ZINC ION, CHLORIDE ION (3 entities in total)
• Functional Keywords: membrane fusion subunit, viral protein
• Biological source: Ebola virus sp.
• Total number of polymer chains: 6
• Total formula weight: 92423.81

Authors

Weissenhorn, W.,Carfi, A.,Lee, K.H.,Skehel, J.J.,Wiley, D.C. (deposition date: 1998-11-03, release date: 1999-07-02, Last modification date: 2024-11-13)

Primary citation

Weissenhorn, W.,Carfi, A.,Lee, K.H.,Skehel, J.J.,Wiley, D.C.
Crystal structure of the Ebola virus membrane fusion subunit, GP2, from the envelope glycoprotein ectodomain.
Mol.Cell, 2:605-616, 1998

PubMed Abstract: We have determined the structure of GP2 from the Ebola virus membrane fusion glycoprotein by X-ray crystallography. The molecule contains a central triple-stranded coiled coil followed by a disulfide-bonded loop homologous to an immunosuppressive sequence in retroviral glycoproteins, which reverses the chain direction and connects to an alpha helix packed antiparallel to the core helices. The structure suggests that fusion peptides near the N termini form disulfide-bonded loops at one end of the molecule and that the C-terminal membrane anchors are at the same end. In this conformation, GP2 could both bridge two membranes and facilitate their apposition to initiate membrane fusion. We also find a heptad irregularity like that in low-pH-induced influenza HA2 and a solvent ion trapped in a coiled coil like that in retroviral TMs.

PubMed: 9844633
DOI: 10.1016/S1097-2765(00)80159-8

Experimental method

X-RAY DIFFRACTION (3 Å)