8BS7

Multimerisation domain of Borna disease virus 1

Summary for 8BS7

• Entry DOI: 10.2210/pdb8bs7/pdb
• Descriptor: Phosphoprotein (1 entity in total)
• Functional Keywords: phosphoprotein, bornavirus, viral protein
• Biological source: Borna disease virus 1
• Total number of polymer chains: 8
• Total formula weight: 196831.30

Authors

Whitehead, J.D.,Grimes, J.M.,Keown, J.R. (deposition date: 2022-11-24, release date: 2023-04-05, Last modification date: 2024-06-19)

Primary citation

Whitehead, J.D.,Grimes, J.M.,Keown, J.R.
Structural and biophysical characterization of the Borna disease virus 1 phosphoprotein.
Acta Crystallogr.,Sect.F, 79:51-60, 2023

PubMed Abstract: Bornaviruses 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 α-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.

PubMed: 36862093
DOI: 10.1107/S2053230X23000717

Experimental method

X-RAY DIFFRACTION (3.2 Å)