5U1C
Structure of tetrameric HIV-1 Strand Transfer Complex Intasome
Summary for 5U1C
Entry DOI | 10.2210/pdb5u1c/pdb |
EMDB information | 8481 8483 |
Descriptor | HIV-1 Integrase, Sso7d chimera, DNA (11-MER), DNA (23-MER), ... (6 entities in total) |
Functional Keywords | integrase, integration, transposase, transesterification, viral protein |
Biological source | Sulfolobus solfataricus More |
Total number of polymer chains | 10 |
Total formula weight | 213018.72 |
Authors | Lyumkis, D.,Passos, D. (deposition date: 2016-11-28, release date: 2017-01-11, Last modification date: 2024-03-13) |
Primary citation | Passos, D.O.,Li, M.,Yang, R.,Rebensburg, S.V.,Ghirlando, R.,Jeon, Y.,Shkriabai, N.,Kvaratskhelia, M.,Craigie, R.,Lyumkis, D. Cryo-EM structures and atomic model of the HIV-1 strand transfer complex intasome. Science, 355:89-92, 2017 Cited by PubMed Abstract: Like all retroviruses, HIV-1 irreversibly inserts a viral DNA (vDNA) copy of its RNA genome into host target DNA (tDNA). The intasome, a higher-order nucleoprotein complex composed of viral integrase (IN) and the ends of linear vDNA, mediates integration. Productive integration into host chromatin results in the formation of the strand transfer complex (STC) containing catalytically joined vDNA and tDNA. HIV-1 intasomes have been refractory to high-resolution structural studies. We used a soluble IN fusion protein to facilitate structural studies, through which we present a high-resolution cryo-electron microscopy (cryo-EM) structure of the core tetrameric HIV-1 STC and a higher-order form that adopts carboxyl-terminal domain rearrangements. The distinct STC structures highlight how HIV-1 can use the common retroviral intasome core architecture to accommodate different IN domain modules for assembly. PubMed: 28059769DOI: 10.1126/science.aah5163 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.9 Å) |
Structure validation
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