6VOY
Cryo-EM structure of HTLV-1 instasome
Summary for 6VOY
Entry DOI | 10.2210/pdb6voy/pdb |
EMDB information | 21301 |
Descriptor | DNA-binding protein 7d, Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform, DNA (5'-D(P*AP*CP*AP*CP*AP*CP*TP*TP*GP*AP*CP*TP*AP*GP*GP*GP*TP*G)-3'), ... (7 entities in total) |
Functional Keywords | integrase, intasome, dna binding protein-dna complex, dna binding protein/dna |
Biological source | Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) More |
Total number of polymer chains | 12 |
Total formula weight | 313413.84 |
Authors | Bhatt, V.,Shi, K.,Sundborger, A.,Aihara, H. (deposition date: 2020-02-01, release date: 2020-07-01, Last modification date: 2024-10-09) |
Primary citation | Bhatt, V.,Shi, K.,Salamango, D.J.,Moeller, N.H.,Pandey, K.K.,Bera, S.,Bohl, T.E.,Kurniawan, F.,Orellana, K.,Zhang, W.,Grandgenett, D.P.,Harris, R.S.,Sundborger-Lunna, A.C.,Aihara, H. Structural basis of host protein hijacking in human T-cell leukemia virus integration. Nat Commun, 11:3121-3121, 2020 Cited by PubMed Abstract: Integration of the reverse-transcribed viral DNA into host chromosomes is a critical step in the life-cycle of retroviruses, including an oncogenic delta(δ)-retrovirus human T-cell leukemia virus type-1 (HTLV-1). Retroviral integrase forms a higher order nucleoprotein assembly (intasome) to catalyze the integration reaction, in which the roles of host factors remain poorly understood. Here, we use cryo-electron microscopy to visualize the HTLV-1 intasome at 3.7-Å resolution. The structure together with functional analyses reveal that the B56γ (B'γ) subunit of an essential host enzyme, protein phosphatase 2 A (PP2A), is repurposed as an integral component of the intasome to mediate HTLV-1 integration. Our studies reveal a key host-virus interaction underlying the replication of an important human pathogen and highlight divergent integration strategies of retroviruses. PubMed: 32561747DOI: 10.1038/s41467-020-16963-6 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.7 Å) |
Structure validation
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