5EJK

Crystal structure of the Rous sarcoma virus intasome

Summary for 5EJK

• Entry DOI: 10.2210/pdb5ejk/pdb
• Descriptor: Gag-Pro-Pol polyprotein, RSV Integrase, DNA (5'-D(*AP*AP*TP*GP*TP*TP*GP*TP*CP*TP*TP*AP*TP*GP*CP*AP*AP*TP*AP*CP*TP*C)-3'), ... (7 entities in total)
• Functional Keywords: rsv, integrase, intasome, transferase-dna complex, transferase/dna
• Biological source: Rous sarcoma virus (strain Prague C) (RSV-PrC); More
• Cellular location: Matrix protein p19: Virion . Capsid protein p27: Virion . Nucleocapsid protein p12: Virion : P03354
• Total number of polymer chains: 16
• Total formula weight: 300817.34

Authors

Yin, Z.,Shi, K.,Banerjee, S.,Aihara, H. (deposition date: 2015-11-02, release date: 2016-02-17, Last modification date: 2024-10-16)

Primary citation

Yin, Z.,Shi, K.,Banerjee, S.,Pandey, K.K.,Bera, S.,Grandgenett, D.P.,Aihara, H.
Crystal structure of the Rous sarcoma virus intasome.
Nature, 530:362-366, 2016

PubMed Abstract: Integration of the reverse-transcribed viral DNA into the host genome is an essential step in the life cycle of retroviruses. Retrovirus integrase catalyses insertions of both ends of the linear viral DNA into a host chromosome. Integrase from HIV-1 and closely related retroviruses share the three-domain organization, consisting of a catalytic core domain flanked by amino- and carboxy-terminal domains essential for the concerted integration reaction. Although structures of the tetrameric integrase-DNA complexes have been reported for integrase from prototype foamy virus featuring an additional DNA-binding domain and longer interdomain linkers, the architecture of a canonical three-domain integrase bound to DNA remained elusive. Here we report a crystal structure of the three-domain integrase from Rous sarcoma virus in complex with viral and target DNAs. The structure shows an octameric assembly of integrase, in which a pair of integrase dimers engage viral DNA ends for catalysis while another pair of non-catalytic integrase dimers bridge between the two viral DNA molecules and help capture target DNA. The individual domains of the eight integrase molecules play varying roles to hold the complex together, making an extensive network of protein-DNA and protein-protein contacts that show both conserved and distinct features compared with those observed for prototype foamy virus integrase. Our work highlights the diversity of retrovirus intasome assembly and provides insights into the mechanisms of integration by HIV-1 and related retroviruses.

PubMed: 26887497
DOI: 10.1038/nature16950

Experimental method

X-RAY DIFFRACTION (3.8 Å)