4JF3

Crystal structure of the mpmv tm retroviral fusion core

4JF3 の概要

• エントリーDOI: 10.2210/pdb4jf3/pdb
• 関連するPDBエントリー: 4JGS 4JPR
• 分子名称: Envelope glycoprotein, CHLORIDE ION (3 entities in total)
• 機能のキーワード: six-helix bundle, fusion, mpmv tm, virus envelope, viral protein
• 由来する生物種: Mason-Pfizer monkey virus (MPMV)
• 細胞内の位置: Transmembrane protein: Virion membrane; Single-pass type I membrane protein (By similarity). Surface protein: Virion membrane; Peripheral membrane protein: P07575
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 22935.98

構造登録者

Cook, J.D.,Aydin, H.,Lee, J.E. (登録日: 2013-02-27, 公開日: 2013-10-23, 最終更新日: 2024-11-20)

主引用文献

Aydin, H.,Cook, J.D.,Lee, J.E.
Crystal structures of Beta- and gammaretrovirus fusion proteins reveal a role for electrostatic stapling in viral entry.
J.Virol., 88:143-153, 2014

PubMed Abstract: Membrane fusion is a key step in the life cycle of all envelope viruses, but this process is energetically unfavorable; the transmembrane fusion subunit (TM) of the virion-attached glycoprotein actively catalyzes the membrane merger process. Retroviral glycoproteins are the prototypical system to study pH-independent viral entry. In this study, we determined crystal structures of extramembrane regions of the TMs from Mason-Pfizer monkey virus (MPMV) and xenotropic murine leukemia virus-related virus (XMRV) at 1.7-Å and 2.2-Å resolution, respectively. The structures are comprised of a trimer of hairpins that is characteristic of class I viral fusion proteins and now completes a structural library of retroviral fusion proteins. Our results allowed us to identify a series of intra- and interchain electrostatic interactions in the heptad repeat and chain reversal regions. Mutagenesis reveals that charge-neutralizing salt bridge mutations significantly destabilize the postfusion six-helix bundle and abrogate retroviral infection, demonstrating that electrostatic stapling of the fusion subunit is essential for viral entry. Our data indicate that salt bridges are a major stabilizing force on the MPMV and XMRV retroviral TMs and likely provide the key energetics for viral and host membrane fusion.

PubMed: 24131724
DOI: 10.1128/JVI.02023-13

実験手法

X-RAY DIFFRACTION (1.7 Å)