1URZ

Low pH induced, membrane fusion conformation of the envelope protein of tick-borne encephalitis virus

1URZ の概要

• エントリーDOI: 10.2210/pdb1urz/pdb
• 関連するPDBエントリー: 1N6G 1SVB
• 分子名称: ENVELOPE PROTEIN (2 entities in total)
• 機能のキーワード: envelope protein, membrane fusion, virus/viral protein, virus-viral protein complex
• 由来する生物種: TICK-BORNE ENCEPHALITIS VIRUS
• 細胞内の位置: Envelope protein E: Virion membrane; Multi- pass membrane protein: Q80E47
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 262738.55

構造登録者

Bressanelli, S.,Rey, F.A. (登録日: 2003-11-16, 公開日: 2004-01-29, 最終更新日: 2024-10-23)

主引用文献

Bressanelli, S.,Stiasny, K.,Allison, S.L.,Stura, E.A.,Duquerroy, S.,Lescar, J.,Heinz, F.X.,Rey, F.A.
Structure of a Flavivirus Envelope Glycoprotein in its Low-Ph-Induced Membrane Fusion Conformation.
Embo J., 23:728-, 2004

PubMed Abstract: Enveloped viruses enter cells via a membrane fusion reaction driven by conformational changes of specific viral envelope proteins. We report here the structure of the ectodomain of the tick-borne encephalitis virus envelope glycoprotein, E, a prototypical class II fusion protein, in its trimeric low-pH-induced conformation. We show that, in the conformational transition, the three domains of the neutral-pH form are maintained but their relative orientation is altered. Similar to the postfusion class I proteins, the subunits rearrange such that the fusion peptide loops cluster at one end of an elongated molecule and the C-terminal segments, connecting to the viral transmembrane region, run along the sides of the trimer pointing toward the fusion peptide loops. Comparison with the low-pH-induced form of the alphavirus class II fusion protein reveals striking differences at the end of the molecule bearing the fusion peptides, suggesting an important conformational effect of the missing membrane connecting segment.

PubMed: 14963486
DOI: 10.1038/SJ.EMBOJ.7600064

実験手法

X-RAY DIFFRACTION (2.7 Å)