8RCQ

Structural flexibility of Nucleoprotein of the Toscana virus in the presence of a nanobody.

Replaces:  8BPK

Summary for 8RCQ

• Entry DOI: 10.2210/pdb8rcq/pdb
• Descriptor: Nucleoprotein, VHH (2 entities in total)
• Functional Keywords: toscana virus, nucleoprotein, saxs, vhh, nanobody, drugs, viral protein
• Biological source: Toscana virus; More
• Total number of polymer chains: 2
• Total formula weight: 42614.51

Authors

Papageorgiou, N.,Ferron, F.,Coutard, B.,Lichiere, J.,Baklouti, A. (deposition date: 2023-12-06, release date: 2024-01-31, Last modification date: 2024-02-14)

Primary citation

Papageorgiou, N.,Baklouti, A.,Lichiere, J.,Desmyter, A.,Canard, B.,Coutard, B.,Ferron, F.
Structural flexibility of Toscana virus nucleoprotein in the presence of a single-chain camelid antibody.
Acta Crystallogr D Struct Biol, 80:113-122, 2024

PubMed Abstract: Phenuiviridae nucleoprotein is the main structural and functional component of the viral cycle, protecting the viral RNA and mediating the essential replication/transcription processes. The nucleoprotein (N) binds the RNA using its globular core and polymerizes through the N-terminus, which is presented as a highly flexible arm, as demonstrated in this article. The nucleoprotein exists in an `open' or a `closed' conformation. In the case of the closed conformation the flexible N-terminal arm folds over the RNA-binding cleft, preventing RNA adsorption. In the open conformation the arm is extended in such a way that both RNA adsorption and N polymerization are possible. In this article, single-crystal X-ray diffraction and small-angle X-ray scattering were used to study the N protein of Toscana virus complexed with a single-chain camelid antibody (VHH) and it is shown that in the presence of the antibody the nucleoprotein is unable to achieve a functional assembly to form a ribonucleoprotein complex.

PubMed: 38265877
DOI: 10.1107/S2059798324000196

Experimental method

X-RAY DIFFRACTION (3.8 Å)