4YXP

The structure of the folded domain of the signature multifunctional protein ICP27 from herpes simplex virus-1 reveals an intertwined dimer.

4YXP の概要

• エントリーDOI: 10.2210/pdb4yxp/pdb
• 分子名称: mRNA export factor, ZINC ION (3 entities in total)
• 機能のキーワード: icp27, herpes simplex virus-1, viral protein
• 由来する生物種: Human herpesvirus 1 (strain 17) (HHV-1)
• 細胞内の位置: Host cytoplasm : P10238
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 60327.86

構造登録者

Tunnicliffe, R.B.,Schacht, M.,Levy, C.W.,Jowitt, T.A.,Sandri-Goldin, R.M.,Golovanov, A.P. (登録日: 2015-03-23, 公開日: 2015-06-17, 最終更新日: 2024-05-08)

主引用文献

Tunnicliffe, R.B.,Schacht, M.,Levy, C.,Jowitt, T.A.,Sandri-Goldin, R.M.,Golovanov, A.P.
The structure of the folded domain from the signature multifunctional protein ICP27 from herpes simplex virus-1 reveals an intertwined dimer.
Sci Rep, 5:11234-11234, 2015

PubMed Abstract: Herpesviruses cause life-long infections by evading the host immune system and establishing latent infections. All mammalian herpesviruses express an essential multifunctional protein that is typified by ICP27 encoded by Herpes Simplex Virus 1. The only region that is conserved among the diverse members of the ICP27 family is a predicted globular domain that has been termed the ICP27 homology domain. Here we present the first crystal structure of the ICP27 homology domain, solved to 1.9 Å resolution. The protein is a homo-dimer, adopting a novel intertwined fold with one CHCC zinc-binding site per monomer. The dimerization, which was independently confirmed by SEC-MALS and AUC, is stabilized by an extensive network of intermolecular contacts, and a domain-swap involving the two N-terminal helices and C-terminal tails. Each monomer contains a lid motif that can clamp the C-terminal tail of its dimeric binding partner against its globular core, without forming any distinct secondary structure elements. The binding interface was probed with point mutations, none of which had a noticeable effect on dimer formation; however deletion of the C-terminal tail region prevented dimer formation in vivo. The structure provides a template for future biochemical studies and modelling of ICP27 homologs from other herpesviruses.

PubMed: 26062451
DOI: 10.1038/srep11234

実験手法

X-RAY DIFFRACTION (1.92 Å)