6PPI

Kaposi's sarcoma-associated herpesvirus (KSHV), C12 portal dodecamer structure

6PPI の概要

• エントリーDOI: 10.2210/pdb6ppi/pdb
• 関連するPDBエントリー: 6PPB 6PPD 6PPH
• EMDBエントリー: 20430 20431 20432 20433 20436 20437
• 分子名称: Portal protein (1 entity in total)
• 機能のキーワード: portal, capsid, genome, genome packaging, virus
• 由来する生物種: Human herpesvirus 8 (HHV-8)
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 817050.19

構造登録者

Gong, D.,Dai, X.,Jih, J.,Liu, Y.T.,Bi, G.Q.,Sun, R.,Zhou, Z.H. (登録日: 2019-07-07, 公開日: 2019-09-11, 最終更新日: 2024-03-20)

主引用文献

Gong, D.,Dai, X.,Jih, J.,Liu, Y.T.,Bi, G.Q.,Sun, R.,Zhou, Z.H.
DNA-Packing Portal and Capsid-Associated Tegument Complexes in the Tumor Herpesvirus KSHV.
Cell, 178:1329-1343.e12, 2019

PubMed Abstract: Assembly of Kaposi's sarcoma-associated herpesvirus (KSHV) begins at a bacteriophage-like portal complex that nucleates formation of an icosahedral capsid with capsid-associated tegument complexes (CATCs) and facilitates translocation of an ∼150-kb dsDNA genome, followed by acquisition of a pleomorphic tegument and envelope. Because of deviation from icosahedral symmetry, KSHV portal and tegument structures have largely been obscured in previous studies. Using symmetry-relaxed cryo-EM, we determined the in situ structure of the KSHV portal and its interactions with surrounding capsid proteins, CATCs, and the terminal end of KSHV's dsDNA genome. Our atomic models of the portal and capsid/CATC, together with visualization of CATCs' variable occupancy and alternate orientation of CATC-interacting vertex triplexes, suggest a mechanism whereby the portal orchestrates procapsid formation and asymmetric long-range determination of CATC attachment during DNA packaging prior to pleomorphic tegumentation/envelopment. Structure-based mutageneses confirm that a triplex deep binding groove for CATCs is a hotspot that holds promise for antiviral development.

PubMed: 31447177
DOI: 10.1016/j.cell.2019.07.035

実験手法

ELECTRON MICROSCOPY (4.7 Å)