1RER

Crystal structure of the homotrimer of fusion glycoprotein E1 from Semliki Forest Virus.

1RER の概要

• エントリーDOI: 10.2210/pdb1rer/pdb
• 関連するPDBエントリー: 1I9W
• 分子名称: Structural polyprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-beta-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[beta-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total)
• 機能のキーワード: envelope glycoprotein, membrane fusion, virus., viral protein
• 由来する生物種: Semliki forest virus
• 細胞内の位置: Capsid protein: Virion . p62: Virion membrane ; Single- pass type I membrane protein . Envelope glycoprotein E2: Virion membrane ; Single-pass type I membrane protein . Envelope glycoprotein E1: Virion membrane ; Single-pass type I membrane protein . Protein 6K: Host cell membrane ; Multi-pass membrane protein : P03315
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 131847.35

構造登録者

Gibbons, D.L.,Vaney, M.C.,Roussel, A.,Vigouroux, A.,Reilly, B.,Kielian, M.,Rey, F.A. (登録日: 2003-11-07, 公開日: 2004-01-27, 最終更新日: 2024-10-16)

主引用文献

Gibbons, D.L.,Vaney, M.C.,Roussel, A.,Vigouroux, A.,Reilly, B.,Lepault, J.,Kielian, M.,Rey, F.A.
Conformational change and protein-protein interactions of the fusion protein of Semliki Forest virus.
Nature, 427:320-325, 2004

PubMed Abstract: 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.

PubMed: 14737160
DOI: 10.1038/nature02239

実験手法

X-RAY DIFFRACTION (3.2 Å)