5OMI

Crystal structure of GP2 from Lassa virus in a post fusion conformation

5OMI の概要

• エントリーDOI: 10.2210/pdb5omi/pdb
• 分子名称: Pre-glycoprotein polyprotein GP complex, CHLORIDE ION, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• 機能のキーワード: viral glycoprotein, viral protein
• 由来する生物種: Lassa mammarenavirus
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 41948.99

構造登録者

Shulman, A.,Diskin, R. (登録日: 2017-07-31, 公開日: 2018-08-29, 最終更新日: 2024-10-23)

主引用文献

Shulman, A.,Katz, M.,Cohen-Dvashi, H.,Greenblatt, H.M.,Levy, Y.,Diskin, R.
Variations in Core Packing of GP2 from Old World Mammarenaviruses in their Post-Fusion Conformations Affect Membrane-Fusion Efficiencies.
J.Mol.Biol., 431:2095-2111, 2019

PubMed Abstract: Lassa virus (LASV) is a notorious human pathogen in West Africa. Its class I trimeric spike complex displays a distinct architecture, and its cell entry mechanism involves unique attributes not shared by other related viruses. We determined the crystal structure of the GP2 fusion glycoprotein from the spike complex of LASV (GP2) in its post-fusion conformation. GP2 adopts a canonical helical bundle configuration similarly to other viruses in its family. The core packing of GP2, however, is more organized compared to GP2 from other viruses reducing the formation of internal hydrophobic cavities. We demonstrate a link between the formation of such unfavorable hydrophobic cavities and the efficiencies of membrane fusion and cell entry. Our study suggests that LASV has evolved a more efficient membrane fusogen compared to other viruses from its family by optimizing the post-fusion configuration of its GP2 module.

PubMed: 31004664
DOI: 10.1016/j.jmb.2019.04.012

実験手法

X-RAY DIFFRACTION (2.56 Å)