4BOM

Structure of herpesvirus fusion glycoprotein B-bilayer complex revealing the protein-membrane and lateral protein-protein interaction

4BOM の概要

• エントリーDOI: 10.2210/pdb4bom/pdb
• EMDBエントリー: 2380
• 分子名称: ENVELOPE GLYCOPROTEIN B (1 entity in total)
• 機能のキーワード: viral protein, membrane proximal region, protein coat, pseudo-atomic virus-host interaction
• 由来する生物種: HUMAN HERPESVIRUS 1 (HUMAN HERPES SIMPLEX VIRUS 1)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 213377.06

構造登録者

Maurer, U.E.,Zeev-Ben-Mordehai, Z.,Pandurangan, A.P.,Cairns, T.M.,Hannah, B.P.,Whitbeck, J.C.,Eisenberg, R.J.,Cohen, G.H.,Topf, M.,Huiskonen, J.T.,Grunewald, K. (登録日: 2013-05-21, 公開日: 2013-07-31, 最終更新日: 2024-05-08)

主引用文献

Maurer, U.E.,Zeev-Ben-Mordehai, T.,Pandurangan, A.P.,Cairns, T.M.,Hannah, B.P.,Whitbeck, J.C.,Eisenberg, R.J.,Cohen, G.H.,Topf, M.,Huiskonen, J.T.,Grunewald, K.
The structure of herpesvirus fusion glycoprotein B-bilayer complex reveals the protein-membrane and lateral protein-protein interaction.
Structure, 21:1396-1405, 2013

PubMed Abstract: Glycoprotein B (gB) is a key component of the complex herpesvirus fusion machinery. We studied membrane interaction of two gB ectodomain forms and present an electron cryotomography structure of the gB-bilayer complex. The two forms differed in presence or absence of the membrane proximal region (MPR) but showed an overall similar trimeric shape. The presence of the MPR impeded interaction with liposomes. In contrast, the MPR-lacking form interacted efficiently with liposomes. Lateral interaction resulted in coat formation on the membranes. The structure revealed that interaction of gB with membranes was mediated by the fusion loops and limited to the outer membrane leaflet. The observed intrinsic propensity of gB to cluster on membranes indicates an additional role of gB in driving the fusion process forward beyond the transient fusion pore opening and subsequently leading to fusion pore expansion.

PubMed: 23850455
DOI: 10.1016/j.str.2013.05.018

実験手法

ELECTRON MICROSCOPY (27 Å)