6CGR

CryoEM structure of herpes simplex virus 1 capsid with associated tegument protein complexes.

これはPDB形式変換不可エントリーです。

6CGR の概要

• エントリーDOI: 10.2210/pdb6cgr/pdb
• EMDBエントリー: 7472
• 分子名称: Major capsid protein, Small capsomere-interacting protein, Triplex capsid protein 1, ... (7 entities in total)
• 機能のキーワード: human herpesvirus 1, herpes simplex virus type 1, capsid-associated tegument complex, virus
• 由来する生物種: Human herpesvirus 1 (HHV-1); 詳細
• タンパク質・核酸の鎖数: 51
• 化学式量合計: 4031743.96

構造登録者

Dai, X.H.,Zhou, Z.H. (登録日: 2018-02-20, 公開日: 2018-03-14, 最終更新日: 2024-11-20)

主引用文献

Dai, X.,Zhou, Z.H.
Structure of the herpes simplex virus 1 capsid with associated tegument protein complexes.
Science, 360:-, 2018

PubMed Abstract: Herpes simplex viruses (HSVs) rely on capsid-associated tegument complex (CATC) for long-range axonal transport of their genome-containing capsids between sites of infection and neuronal cell bodies. Here we report cryo-electron microscopy structures of the HSV-1 capsid with CATC up to 3.5-angstrom resolution and atomic models of multiple conformers of capsid proteins VP5, VP19c, VP23, and VP26 and tegument proteins pUL17, pUL25, and pUL36. Crowning every capsid vertex are five copies of heteropentameric CATC, each containing a pUL17 monomer supporting the coiled-coil helix bundle of a pUL25 dimer and a pUL36 dimer, thus positioning their flexible domains for potential involvement in nuclear capsid egress and axonal capsid transport. Notwithstanding newly discovered fold conservation between triplex proteins and bacteriophage λ protein gpD and the previously recognized bacteriophage HK97 gp5-like fold in VP5, HSV-1 capsid proteins exhibit extraordinary diversity in forms of domain insertion and conformational polymorphism, not only for interactions with tegument proteins but also for encapsulation of large genomes.

PubMed: 29622628
DOI: 10.1126/science.aao7298

実験手法

ELECTRON MICROSCOPY (4.2 Å)