2M5F

NMR Structure of the Complete Internal Fusion Loop mutant L529A/I544A from Ebolavirus GP2 at pH 5.5

2M5F の概要

• エントリーDOI: 10.2210/pdb2m5f/pdb
• NMR情報: BMRB: 19052
• 分子名称: Virion spike glycoprotein (1 entity in total)
• 機能のキーワード: ebolavirus, fusion loop, double mutant l529a/i544a, viral protein
• 由来する生物種: Zaire ebolavirus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 5863.53

構造登録者

Gregory, S.M.,Tamm, L.K. (登録日: 2013-02-22, 公開日: 2014-02-26, 最終更新日: 2024-11-20)

主引用文献

Gregory, S.M.,Larsson, P.,Nelson, E.A.,Kasson, P.M.,White, J.M.,Tamm, L.K.
Ebolavirus Entry Requires a Compact Hydrophobic Fist at the Tip of the Fusion Loop.
J.Virol., 88:6636-6649, 2014

PubMed Abstract: Ebolavirus is an enveloped virus causing severe hemorrhagic fever. Its surface glycoproteins undergo proteolytic cleavage and rearrangements to permit membrane fusion and cell entry. Here we focus on the glycoprotein's internal fusion loop (FL), critical for low-pH-triggered fusion in the endosome. Alanine mutations at L529 and I544 and particularly the L529 I544 double mutation compromised viral entry and fusion. The nuclear magnetic resonance (NMR) structures of the I544A and L529A I544A mutants in lipid environments showed significant disruption of a three-residue scaffold that is required for the formation of a consolidated fusogenic hydrophobic surface at the tip of the FL. Biophysical experiments and molecular simulation revealed the position of the wild-type (WT) FL in membranes and showed the inability of the inactive double mutant to reach this position. Consolidation of hydrophobic residues at the tip of FLs may be a common requirement for internal FLs of class I, II, and III fusion proteins.

PubMed: 24696482
DOI: 10.1128/JVI.00396-14

実験手法

SOLUTION NMR