7SEP

Cryo-EM Structure of the RT component of the HIV-1 Pol Polyprotein

7SEP の概要

• エントリーDOI: 10.2210/pdb7sep/pdb
• EMDBエントリー: 25074
• 分子名称: Gag-Pol polyprotein (1 entity in total)
• 機能のキーワード: hiv-1, viral protein, enzyme, transferase, hydrolase
• 由来する生物種: Human immunodeficiency virus type 1 BH10
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 238579.73

構造登録者

Lyumkis, D.,Passos, D.,Arnold, E.,Harrison, J.J.E. (登録日: 2021-10-01, 公開日: 2022-07-27, 最終更新日: 2024-06-05)

主引用文献

Harrison, J.J.E.K.,Passos, D.O.,Bruhn, J.F.,Bauman, J.D.,Tuberty, L.,DeStefano, J.J.,Ruiz, F.X.,Lyumkis, D.,Arnold, E.
Cryo-EM structure of the HIV-1 Pol polyprotein provides insights into virion maturation.
Sci Adv, 8:eabn9874-eabn9874, 2022

PubMed Abstract: Key proteins of retroviruses and other RNA viruses are translated and subsequently processed from polyprotein precursors by the viral protease (PR). Processing of the HIV Gag-Pol polyprotein yields the HIV structural proteins and enzymes. Structures of the mature enzymes PR, reverse transcriptase (RT), and integrase (IN) aided understanding of catalysis and design of antiretrovirals, but knowledge of the Pol precursor architecture and function before PR cleavage is limited. We developed a system to produce stable HIV-1 Pol and determined its cryo-electron microscopy structure. RT in Pol has a similar arrangement to the mature RT heterodimer, and its dimerization may draw together two PR monomers to activate proteolytic processing. HIV-1 thus may leverage the dimerization interfaces in Pol to regulate assembly and maturation of polyprotein precursors.

PubMed: 35857464
DOI: 10.1126/sciadv.abn9874

実験手法

ELECTRON MICROSCOPY (3.8 Å)