1rer
From Proteopedia
|
Crystal structure of the homotrimer of fusion glycoprotein E1 from Semliki Forest Virus.
Overview
Fusion of biological membranes is mediated by specific lipid-interacting, proteins that induce the formation and expansion of an initial fusion, pore. Here we report the crystal structure of the ectodomain of the, Semliki Forest virus fusion glycoprotein E1 in its low-pH-induced trimeric, form. E1 adopts a folded-back conformation that, in the final post-fusion, form of the full-length protein, would bring the fusion peptide loop and, the transmembrane anchor to the same end of a stable protein rod. The, observed conformation of the fusion peptide loop is compatible with, interactions only with the outer leaflet of the lipid bilayer. Crystal, contacts between fusion peptide loops of adjacent E1 trimers, together, with electron microscopy observations, suggest that in an early step of, membrane fusion, an intermediate assembly of five trimers creates two, opposing nipple-like deformations in the viral and target membranes, leading to formation of the fusion pore.
About this Structure
1RER is a Single protein structure of sequence from Semliki forest virus with PO4, BR and HO as ligands. Full crystallographic information is available from OCA.
Reference
Conformational change and protein-protein interactions of the fusion protein of Semliki Forest virus., Gibbons DL, Vaney MC, Roussel A, Vigouroux A, Reilly B, Lepault J, Kielian M, Rey FA, Nature. 2004 Jan 22;427(6972):320-5. PMID:14737160
Page seeded by OCA on Wed Nov 21 01:32:02 2007
Categories: Semliki forest virus | Single protein | Gibbons, D.L. | Kielian, M. | Reilly, B. | Rey, F.A. | Roussel, A. | Vaney, M.C. | Vigouroux, A. | BR | HO | PO4 | Envelope glycoprotein | Membrane fusion | Virus.
