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5U1C

Structure of tetrameric HIV-1 Strand Transfer Complex Intasome

Summary for 5U1C
Entry DOI10.2210/pdb5u1c/pdb
EMDB information8481 8483
DescriptorHIV-1 Integrase, Sso7d chimera, DNA (11-MER), DNA (23-MER), ... (6 entities in total)
Functional Keywordsintegrase, integration, transposase, transesterification, viral protein
Biological sourceSulfolobus solfataricus
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Total number of polymer chains10
Total formula weight213018.72
Authors
Lyumkis, D.,Passos, D. (deposition date: 2016-11-28, release date: 2017-01-11, Last modification date: 2024-03-13)
Primary citationPassos, 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: 28059769
DOI: 10.1126/science.aah5163
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.9 Å)
Structure validation

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