3U3I

A RNA binding protein from Crimean-Congo hemorrhagic fever virus

Summary for 3U3I

• Entry DOI: 10.2210/pdb3u3i/pdb
• Descriptor: Nucleocapsid protein (2 entities in total)
• Functional Keywords: nucleocapsid protein, endonuclease, rna binding, cchfv, rna binding protein
• Biological source: Crimean-Congo hemorrhagic fever virus
• Total number of polymer chains: 1
• Total formula weight: 53984.30

Authors

Guo, Y.,Wang, W.M.,Ji, W.,Deng, M.,Sun, Y.N.,Lou, Z.Y.,Rao, Z.H. (deposition date: 2011-10-06, release date: 2012-03-28, Last modification date: 2024-03-20)

Primary citation

Guo, Y.,Wang, W.M.,Ji, W.,Deng, M.,Sun, Y.N.,Zhou, H.,Yang, C.,Deng, F.,Wang, H.,Hu, Z.,Lou, Z.Y.,Rao, Z.H.
Crimean-Congo hemorrhagic fever virus nucleoprotein reveals endonuclease activity in bunyaviruses
Proc.Natl.Acad.Sci.USA, 109:5046-5051, 2012

PubMed Abstract: Crimean-Congo hemorrhagic fever virus (CCHFV), a virus with high mortality in humans, is a member of the genus Nairovirus in the family Bunyaviridae, and is a causative agent of severe hemorrhagic fever (HF). It is classified as a biosafety level 4 pathogen and a potential bioterrorism agent due to its aerosol infectivity and its ability to cause HF outbreaks with high case fatality (∼30%). However, little is known about the structural features and function of nucleoproteins (NPs) in the Bunyaviridae, especially in CCHFV. Here we report a 2.3-Å resolution crystal structure of the CCHFV nucleoprotein. The protein has a racket-shaped overall structure with distinct "head" and "stalk" domains and differs significantly with NPs reported so far from other negative-sense single-stranded RNA viruses. Furthermore, CCHFV NP shows a distinct metal-dependent DNA-specific endonuclease activity. Single residue mutations in the predicted active site resulted in a significant reduction in the observed endonuclease activity. Our results present a new folding mechanism and function for a negative-strand RNA virus nucleoprotein, extend our structural insight into bunyavirus NPs, and provide a potential target for antiviral drug development to treat CCHFV infection.

PubMed: 22421137
DOI: 10.1073/pnas.1200808109

Experimental method

X-RAY DIFFRACTION (2.304 Å)