7ZPP

Cryo-EM structure of the MVV CSC intasome at 4.5A resolution

Replaces:  5M0Q

Summary for 7ZPP

• Entry DOI: 10.2210/pdb7zpp/pdb
• EMDB information: 14860
• Descriptor: Integrase, vDNA, non-transferred strand, vDNA, transferred strand (3 entities in total)
• Functional Keywords: integrase, intasome, mvv, nucleoprotein complex, retrovirus, viral protein
• Biological source: Visna/maedi virus EV1 KV1772; More
• Total number of polymer chains: 20
• Total formula weight: 542445.03

Authors

Ballandras-Colas, A.,Maskell, D.,Pye, V.E.,Locke, J.,Swuec, S.,Kotecha, A.,Costa, A.,Cherepanov, P. (deposition date: 2022-04-28, release date: 2022-05-11, Last modification date: 2024-07-24)

Primary citation

Ballandras-Colas, A.,Maskell, D.P.,Serrao, E.,Locke, J.,Swuec, P.,Jonsson, S.R.,Kotecha, A.,Cook, N.J.,Pye, V.E.,Taylor, I.A.,Andresdottir, V.,Engelman, A.N.,Costa, A.,Cherepanov, P.
A supramolecular assembly mediates lentiviral DNA integration
Science, 355:93-95, 2017

PubMed Abstract: Retroviral integrase (IN) functions within the intasome nucleoprotein complex to catalyze insertion of viral DNA into cellular chromatin. Using cryo-electron microscopy, we now visualize the functional maedi-visna lentivirus intasome at 4.9 angstrom resolution. The intasome comprises a homo-hexadecamer of IN with a tetramer-of-tetramers architecture featuring eight structurally distinct types of IN protomers supporting two catalytically competent subunits. The conserved intasomal core, previously observed in simpler retroviral systems, is formed between two IN tetramers, with a pair of C-terminal domains from flanking tetramers completing the synaptic interface. Our results explain how HIV-1 IN, which self-associates into higher-order multimers, can form a functional intasome, reconcile the bulk of early HIV-1 IN biochemical and structural data, and provide a lentiviral platform for design of HIV-1 IN inhibitors.

PubMed: 28059770
DOI: 10.1126/science.aah7002

Experimental method

ELECTRON MICROSCOPY (4.5 Å)