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6VOY

Cryo-EM structure of HTLV-1 instasome

Summary for 6VOY
Entry DOI10.2210/pdb6voy/pdb
EMDB information21301
DescriptorDNA-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 Keywordsintegrase, intasome, dna binding protein-dna complex, dna binding protein/dna
Biological sourceSaccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
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Total number of polymer chains12
Total formula weight313413.84
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 citationBhatt, 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: 32561747
DOI: 10.1038/s41467-020-16963-6
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.7 Å)
Structure validation

226707

数据于2024-10-30公开中

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