5LLJ
Maedi-Visna virus (MVV) integrase C-terminal domain (residues 220-276)
Summary for 5LLJ
| Entry DOI | 10.2210/pdb5llj/pdb |
| Descriptor | Integrase, CHLORIDE ION (3 entities in total) |
| Functional Keywords | integrase, visna/maedi virus, c-terminal domain, viral protein |
| Biological source | Maedi visna virus (strain KV1772) (MVV) |
| Total number of polymer chains | 2 |
| Total formula weight | 13491.00 |
| Authors | Pye, V.E.,Maskell, D.P.,Cherepanov, P. (deposition date: 2016-07-27, release date: 2017-01-18, Last modification date: 2024-01-10) |
| Primary citation | Ballandras-Colas, A.,Maskell, D.P.,Serrao, E.,Locke, J.,Swuec, P.,Jonsson, S.R.,Kotecha, A.,Cook, N.J.,Pye, V.E.,Taylor, I.A.,Andresdottir, V.,Engelman, A.N.,Costa, A.,Cherepanov, P. A supramolecular assembly mediates lentiviral DNA integration. Science, 355:93-95, 2017 Cited by PubMed Abstract: Retroviral integrase (IN) functions within the intasome nucleoprotein complex to catalyze insertion of viral DNA into cellular chromatin. Using cryo-electron microscopy, we now visualize the functional maedi-visna lentivirus intasome at 4.9 angstrom resolution. The intasome comprises a homo-hexadecamer of IN with a tetramer-of-tetramers architecture featuring eight structurally distinct types of IN protomers supporting two catalytically competent subunits. The conserved intasomal core, previously observed in simpler retroviral systems, is formed between two IN tetramers, with a pair of C-terminal domains from flanking tetramers completing the synaptic interface. Our results explain how HIV-1 IN, which self-associates into higher-order multimers, can form a functional intasome, reconcile the bulk of early HIV-1 IN biochemical and structural data, and provide a lentiviral platform for design of HIV-1 IN inhibitors. PubMed: 28059770DOI: 10.1126/science.aah7002 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.78 Å) |
Structure validation
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