6Z9M

Pseudoatomic model of the pre-fusion conformation of glycoprotein B of Herpes simplex virus 1

「5FZ2」から置き換えられました

6Z9M の概要

• エントリーDOI: 10.2210/pdb6z9m/pdb
• EMDBエントリー: 11123 3362
• 分子名称: Envelope glycoprotein B (1 entity in total)
• 機能のキーワード: membrane fusion protein, glycoprotein, gb, ul27, viral entry protein, class iii fusion protein, transmembrane protein, pre-fusion conformation, viral protein
• 由来する生物種: Human herpesvirus 1 (HHV-1)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 301149.91

構造登録者

Vollmer, B.,Prazak, V.,Vasishtan, D.,Jefferys, E.E.,Hernandez-Duran, A.,Vallbracht, M.,Klupp, B.,Mettenleiter, T.C.,Backovic, M.,Rey, F.A.,Topf, M.,Gruenewald, K. (登録日: 2020-06-04, 公開日: 2020-10-07, 最終更新日: 2020-10-14)

主引用文献

Vollmer, B.,Prazak, V.,Vasishtan, D.,Jefferys, E.E.,Hernandez-Duran, A.,Vallbracht, M.,Klupp, B.G.,Mettenleiter, T.C.,Backovic, M.,Rey, F.A.,Topf, M.,Grunewald, K.
The prefusion structure of herpes simplex virus glycoprotein B.
Sci Adv, 6:-, 2020

PubMed Abstract: Cell entry of enveloped viruses requires specialized viral proteins that mediate fusion with the host membrane by substantial structural rearrangements from a metastable pre- to a stable postfusion conformation. This metastability renders the herpes simplex virus 1 (HSV-1) fusion glycoprotein B (gB) highly unstable such that it readily converts into the postfusion form, thereby precluding structural elucidation of the pharmacologically relevant prefusion conformation. By identification of conserved sequence signatures and molecular dynamics simulations, we devised a mutation that stabilized this form. Functionally locking gB allowed the structural determination of its membrane-embedded prefusion conformation at sub-nanometer resolution and enabled the unambiguous fit of all ectodomains. The resulting pseudo-atomic model reveals a notable conservation of conformational domain rearrangements during fusion between HSV-1 gB and the vesicular stomatitis virus glycoprotein G, despite their very distant phylogeny. In combination with our comparative sequence-structure analysis, these findings suggest common fusogenic domain rearrangements in all class III viral fusion proteins.

PubMed: 32978151
DOI: 10.1126/sciadv.abc1726

実験手法

ELECTRON MICROSCOPY (9.1 Å)