6I2N
Helical RNA-bound Hantaan virus nucleocapsid
Summary for 6I2N
Entry DOI | 10.2210/pdb6i2n/pdb |
EMDB information | 0333 |
Descriptor | RNA (5'-R(P*UP*UP*U)-3'), Nucleoprotein (2 entities in total) |
Functional Keywords | nucleoprotein, nucleocapsid, rna-binding, viral protein |
Biological source | Hantaan orthohantavirus (Korean hemorrhagic fever virus) More |
Total number of polymer chains | 2 |
Total formula weight | 49135.81 |
Authors | Arragain, B.,Reguera, J.,Desfosses, A.,Gutsche, I.,Schoehn, G.,Malet, H. (deposition date: 2018-11-01, release date: 2019-01-23, Last modification date: 2024-05-15) |
Primary citation | Arragain, B.,Reguera, J.,Desfosses, A.,Gutsche, I.,Schoehn, G.,Malet, H. High resolution cryo-EM structure of the helical RNA-bound Hantaan virus nucleocapsid reveals its assembly mechanisms. Elife, 8:-, 2019 Cited by PubMed 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 characterisation at high resolution. Here, we describe purification of full-length recombinant metastable helical nucleocapsid of Hantaan virus ( family, order) and determine its structure at 3.3 Å resolution by cryo-electron microscopy. The structure reveals the mechanisms of helical multimerisation 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. PubMed: 30638449DOI: 10.7554/eLife.43075 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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