4FG0

Structure of the St. Louis Encephalitis Virus envelope protein in the fusogenic trimer conformation.

4FG0 の概要

• エントリーDOI: 10.2210/pdb4fg0/pdb
• 関連するPDBエントリー: 1OK8 1RER 1URZ 3G7T
• 分子名称: Polyprotein (1 entity in total)
• 機能のキーワード: viral envelope proteins, structural genomics, fusion peptide, antibody epitopes, flavivirus, st. louis encephalitis virus, niaid, national institute of allergy and infectious diseases, center for structural genomics of infectious diseases, csgid, viral protein
• 由来する生物種: St. Louis encephalitis virus
• 細胞内の位置: Host endoplasmic reticulum membrane ; Multi-pass membrane protein . Host endoplasmic reticulum membrane ; Peripheral membrane protein ; Cytoplasmic side . Host endoplasmic reticulum membrane ; Peripheral membrane protein ; Lumenal side . Host nucleus . Secreted . Virion membrane ; Multi-pass membrane protein : Q9ENF3
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 44614.00

構造登録者

Luca, V.C.,Nelson, C.A.,Fremont, D.H.,Center for Structural Genomics of Infectious Diseases (CSGID) (登録日: 2012-06-01, 公開日: 2012-06-27, 最終更新日: 2024-11-27)

主引用文献

Luca, V.C.,Nelson, C.A.,Fremont, D.H.
Structure of the st. Louis encephalitis virus postfusion envelope trimer.
J.Virol., 87:818-828, 2013

PubMed Abstract: St. Louis encephalitis virus (SLEV) is a mosquito-borne flavivirus responsible for several human encephalitis outbreaks over the last 80 years. Mature flavivirus virions are coated with dimeric envelope (E) proteins that mediate attachment and fusion with host cells. E is a class II fusion protein, the hallmark of which is a distinct dimer-to-trimer rearrangement that occurs upon endosomal acidification and insertion of hydrophobic fusion peptides into the endosomal membrane. Herein, we report the crystal structure of SLEV E in the posfusion trimer conformation. The structure revealed specific features that differentiate SLEV E from trimers of related flavi- and alphaviruses. SLEV E fusion loops have distinct intermediate spacing such that they are positioned further apart than previously observed in flaviviruses but closer together than Semliki Forest virus, an alphavirus. Domains II and III (DII and DIII) of SLEV E also adopt different angles relative to DI, which suggests that the DI-DII joint may accommodate spheroidal motions. However, trimer interfaces are well conserved among flaviviruses, so it is likely the differences observed represent structural features specific to SLEV function. Analysis of surface potentials revealed a basic platform underneath flavivirus fusion loops that may interact with the anionic lipid head groups found in membranes. Taken together, these results highlight variations in E structure and assembly that may direct virus-specific interactions with host determinants to influence pathogenesis.

PubMed: 23115296
DOI: 10.1128/JVI.01950-12

実験手法

X-RAY DIFFRACTION (3.899 Å)