Summary information and primary citation
- PDB-id
- 6i2n; DSSR-derived features in text and JSON formats
- Class
- viral protein
- Method
- cryo-EM (3.3 Å)
- Summary
- Helical RNA-bound hantaan virus nucleocapsid
- Reference
- Arragain B, Reguera J, Desfosses A, Gutsche I, Schoehn G, Malet H (2019): "High resolution cryo-EM structure of the helical RNA-bound Hantaan virus nucleocapsid reveals its assembly mechanisms." Elife, 8. doi: 10.7554/eLife.43075.
- Abstract
- Negative-strand RNA viruses condense their genome into helical nucleocapsids that constitute essential templates for viral replication and transcription. The intrinsic flexibility of nucleocapsids usually prevents their full-length structural characterization at high resolution. Here we describe purification of full-length recombinant metastable helical nucleocapsid of Hantaan virus (Hantaviridae family, Bunyavirales order) and determine its structure at 3.3 Å resolution by cryo-electron microscopy. The structure reveals the mechanisms of helical multimerization via sub-domain exchanges between protomers and highlights nucleotide positions in a continuous positively charged groove compatible with viral genome binding. It uncovers key sites for future structure-based design of antivirals that are currently lacking to counteract life-threatening hantavirus infections. The structure also suggests a model of nucleoprotein-polymerase interaction that would enable replication and transcription solely upon local disruption of the nucleocapsid.
