1rer

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spinqualitylabelsall models PDB ID 1rer Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
, resolution 3.2Å
Ligands:	, and
Coordinates:	save as pdb, mmCIF, xml

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. 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

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