5HUW

Structure of HSV-1 Large Terminase NLS bound to importin alpha

5HUW の概要

• エントリーDOI: 10.2210/pdb5huw/pdb
• 関連するPDBエントリー: 3Q5U
• 分子名称: Importin subunit alpha-1, HSV1 large terminase NLS (3 entities in total)
• 機能のキーワード: nuclear import, nls, importin alpha-1, herpes virus, viral protein, tranport protein
• 由来する生物種: Mus musculus (Mouse); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 60395.64

構造登録者

Sankhala, R.S.,Lokareddy, R.K.,Cingolani, G. (登録日: 2016-01-27, 公開日: 2016-03-09, 最終更新日: 2023-09-27)

主引用文献

Sankhala, R.S.,Lokareddy, R.K.,Cingolani, G.
Divergent Evolution of Nuclear Localization Signal Sequences in Herpesvirus Terminase Subunits.
J.Biol.Chem., 291:11420-11433, 2016

PubMed Abstract: The tripartite terminase complex of herpesviruses assembles in the cytoplasm of infected cells and exploits the host nuclear import machinery to gain access to the nucleus, where capsid assembly and genome-packaging occur. Here we analyzed the structure and conservation of nuclear localization signal (NLS) sequences previously identified in herpes simplex virus 1 (HSV-1) large terminase and human cytomegalovirus (HCMV) small terminase. We found a monopartite NLS at the N terminus of large terminase, flanking the ATPase domain, that is conserved only in α-herpesviruses. In contrast, small terminase exposes a classical NLS at the far C terminus of its helical structure that is conserved only in two genera of the β-subfamily and absent in α- and γ-herpesviruses. In addition, we predicted a classical NLS in the third terminase subunit that is partially conserved among herpesviruses. Bioinformatic analysis revealed that both location and potency of NLSs in terminase subunits evolved more rapidly than the rest of the amino acid sequence despite the selective pressure to keep terminase gene products active and localized in the nucleus. We propose that swapping NLSs among terminase subunits is a regulatory mechanism that allows different herpesviruses to regulate the kinetics of terminase nuclear import, reflecting a mechanism of virus:host adaptation.

PubMed: 27033706
DOI: 10.1074/jbc.M116.724393

実験手法

X-RAY DIFFRACTION (1.95 Å)