3MWT

Crystal structure of Lassa fever virus nucleoprotein in complex with Mn2+

Summary for 3MWT

• Entry DOI: 10.2210/pdb3mwt/pdb
• Related: 3MWP 3MX2 3MX5
• Descriptor: Nucleoprotein, MANGANESE (II) ION, ZINC ION, ... (4 entities in total)
• Functional Keywords: nucleoprotein, lassa fever virus, structural genomics, scottish structural proteomics facility, sspf, nuclear protein
• Biological source: Lassa virus (LASV)
• Cellular location: Virion: P13699
• Total number of polymer chains: 3
• Total formula weight: 192256.48

Authors

Qi, X.,Lan, S.,Wang, W.,Schelde, L.M.,Dong, H.,Wallat, G.,Liang, Y.,Ly, H.,Dong, C.,Scottish Structural Proteomics Facility (SSPF) (deposition date: 2010-05-06, release date: 2010-12-01, Last modification date: 2023-09-06)

Primary citation

Qi, X.,Lan, S.,Wang, W.,Schelde, L.M.,Dong, H.,Wallat, G.D.,Ly, H.,Liang, Y.,Dong, C.
Cap binding and immune evasion revealed by Lassa nucleoprotein structure.
Nature, 468:779-783, 2010

PubMed Abstract: Lassa virus, the causative agent of Lassa fever, causes thousands of deaths annually and is a biological threat agent, for which there is no vaccine and limited therapy. The nucleoprotein (NP) of Lassa virus has essential roles in viral RNA synthesis and immune suppression, the molecular mechanisms of which are poorly understood. Here we report the crystal structure of Lassa virus NP at 1.80 Å resolution, which reveals amino (N)- and carboxy (C)-terminal domains with structures unlike any of the reported viral NPs. The N domain folds into a novel structure with a deep cavity for binding the m7GpppN cap structure that is required for viral RNA transcription, whereas the C domain contains 3'-5' exoribonuclease activity involved in suppressing interferon induction. To our knowledge this is the first X-ray crystal structure solved for an arenaviral NP, which reveals its unexpected functions and indicates unique mechanisms in cap binding and immune evasion. These findings provide great potential for vaccine and drug development.

PubMed: 21085117
DOI: 10.1038/nature09605

Experimental method

X-RAY DIFFRACTION (1.982 Å)