6P59
Crystal structure of SIVrcm Vif-CBFbeta-ELOB-ELOC complex
Summary for 6P59
| Entry DOI | 10.2210/pdb6p59/pdb |
| Descriptor | Core-binding factor subunit beta, Elongin-B, Elongin-C, ... (8 entities in total) |
| Functional Keywords | complex, vif, a3g, viral protein, viral protein-immune system complex, viral protein/immune system |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 8 |
| Total formula weight | 142429.32 |
| Authors | Binning, J.M.,Chesarino, N.M.,Emerman, M.,Gross, J.D. (deposition date: 2019-05-29, release date: 2019-12-25, Last modification date: 2023-10-11) |
| Primary citation | Binning, J.M.,Chesarino, N.M.,Emerman, M.,Gross, J.D. Structural Basis for a Species-Specific Determinant of an SIV Vif Protein toward Hominid APOBEC3G Antagonism. Cell Host Microbe, 26:739-747.e4, 2019 Cited by PubMed Abstract: Primate lentiviruses encode a Vif protein that counteracts the host antiviral APOBEC3 (A3) family members. The adaptation of Vif to species-specific A3 determinants is a critical event that allowed the spillover of a lentivirus from monkey reservoirs to chimpanzees and subsequently to humans, which gave rise to HIV-1 and the acquired immune deficiency syndrome (AIDS) pandemic. How Vif-A3 protein interactions are remodeled during evolution is unclear. Here, we report a 2.94 Å crystal structure of the Vif substrate receptor complex from simian immunodeficiency virus isolated from red-capped mangabey (SIVrcm). The structure of the SIVrcm Vif complex illuminates the stage of lentiviral Vif evolution that is immediately prior to entering hominid primates. Structure-function studies reveal the adaptations that allowed SIVrcm Vif to antagonize hominid A3G. These studies show a partitioning between an evolutionarily dynamic specificity determinant and a conserved protein interacting surface on Vif that enables adaptation while maintaining protein interactions required for potent A3 antagonism. PubMed: 31830442DOI: 10.1016/j.chom.2019.10.014 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.94221405643 Å) |
Structure validation
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