4TT0

Crystal structure of fragment 1600-1733 of HSV1 UL36 in the presence of 1M potassium iodide

4TT0 の概要

• エントリーDOI: 10.2210/pdb4tt0/pdb
• 分子名称: Deneddylase, IODIDE ION (3 entities in total)
• 機能のキーワード: hydrolase, fibrous protein tegument protein
• 由来する生物種: Human herpesvirus 1(type 1 / strain 17) (HHV-1)
• 細胞内の位置: Virion tegument: P10220
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 35262.27

構造登録者

Scrima, N.,Bressanelli, S.,Roche, S. (登録日: 2014-06-19, 公開日: 2015-02-18, 最終更新日: 2024-05-08)

主引用文献

Scrima, N.,Lepault, J.,Boulard, Y.,Pasdeloup, D.,Bressanelli, S.,Roche, S.
Insights into Herpesvirus Tegument Organization from Structural Analyses of the 970 Central Residues of HSV-1 UL36 Protein.
J.Biol.Chem., 290:8820-8833, 2015

PubMed Abstract: The tegument of all herpesviruses contains a capsid-bound large protein that is essential for multiple viral processes, including capsid transport, decapsidation at the nuclear pore complex, particle assembly, and secondary envelopment, through mechanisms that are still incompletely understood. We report here a structural characterization of the central 970 residues of this protein for herpes simplex virus type 1 (HSV-1 UL36, 3164 residues). This large fragment is essentially a 34-nm-long monomeric fiber. The crystal structure of its C terminus shows an elongated domain-swapped dimer. Modeling and molecular dynamics simulations give a likely molecular organization for the monomeric form and extend our findings to alphaherpesvirinae. Hence, we propose that an essential feature of UL36 is the existence in its central region of a stalk capable of connecting capsid and membrane across the tegument and that the ability to switch between monomeric and dimeric forms may help UL36 fulfill its multiple functions.

PubMed: 25678705
DOI: 10.1074/jbc.M114.612838

実験手法

X-RAY DIFFRACTION (2.599 Å)