8bs7 | pdb_00008bs7
Multimerisation domain of Borna disease virus 1
Structural highlights
FunctionPHOSP_BDVV Essential component of the RNA polymerase transcription and replication complex. Acts as a scaffold which brings L in close proximity to the N-RNA complex. Plays a role in the segregation of the viral genome in host daughter cells during mitosis by interacting with host HMGB1, a host chromatin-remodeling DNA architectural protein, thereby stabilizing RNP on chromosomes. Interacts with host TBK1 and thus interferes with activation of cellular antiviral state. Inhibits cellular histone acetyltransferase activities.[UniProtKB:P0C798][1] [2] [3] Publication Abstract from PubMedBornaviruses are RNA viruses with a mammalian, reptilian, and avian host range. The viruses infect neuronal cells and in rare cases cause a lethal encephalitis. The family Bornaviridae are part of the Mononegavirales order of viruses, which contain a nonsegmented viral genome. Mononegavirales encode a viral phosphoprotein (P) that binds both the viral polymerase (L) and the viral nucleoprotein (N). The P protein acts as a molecular chaperone and is required for the formation of a functional replication/transcription complex. In this study, the structure of the oligomerization domain of the phosphoprotein determined by X-ray crystallography is reported. The structural results are complemented with biophysical characterization using circular dichroism, differential scanning calorimetry and small-angle X-ray scattering. The data reveal the phosphoprotein to assemble into a stable tetramer, with the regions outside the oligomerization domain remaining highly flexible. A helix-breaking motif is observed between the alpha-helices at the midpoint of the oligomerization domain that appears to be conserved across the Bornaviridae. These data provide information on an important component of the bornavirus replication complex. Structural and biophysical characterization of the Borna disease virus 1 phosphoprotein.,Whitehead JD, Grimes JM, Keown JR Acta Crystallogr F Struct Biol Commun. 2023 Mar 1;79(Pt 3):51-60. doi: , 10.1107/S2053230X23000717. Epub 2023 Feb 23. PMID:36862093[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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