7SEP

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

Summary for 7SEP

• Entry DOI: 10.2210/pdb7sep/pdb
• EMDB information: 25074
• Descriptor: Gag-Pol polyprotein (1 entity in total)
• Functional Keywords: hiv-1, viral protein, enzyme, transferase, hydrolase
• Biological source: Human immunodeficiency virus type 1 BH10
• Total number of polymer chains: 2
• Total formula weight: 238579.73

Authors

Lyumkis, D.,Passos, D.,Arnold, E.,Harrison, J.J.E. (deposition date: 2021-10-01, release date: 2022-07-27, Last modification date: 2024-06-05)

Primary citation

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

Experimental method

ELECTRON MICROSCOPY (3.8 Å)