Actions for Structure of the paramyxovirus parainfluenza virus 5 nucleoprotein–RNA complex [electronic resource].

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Structure of the paramyxovirus parainfluenza virus 5 nucleoprotein–RNA complex [electronic resource].

Published
Washington, D.C. : United States. Dept. of Energy. Office of Basic Energy Sciences, 2015.
Oak Ridge, Tenn. : Distributed by the Office of Scientific and Technical Information, U.S. Dept. of Energy
Physical Description
pages E1,792-E1,799 : digital, PDF file
Additional Creators
United States. Department of Energy. Office of Basic Energy Sciences and United States. Department of Energy. Office of Scientific and Technical Information
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Summary
Parainfluenza virus 5 (PIV5) is a member of the Paramyxoviridae family of membrane-enveloped viruses with a negative-sense RNA genome that is packaged and protected by long filamentous nucleocapsid-helix structures (RNPs). These RNPs, consisting of ~2,600 protomers of nucleocapsid (N) protein, form the template for viral transcription and replication. In this paper, we have determined the 3D X-ray crystal structure of the nucleoprotein (N)-RNA complex from PIV5 to 3.11-Å resolution. The structure reveals a 13-mer nucleocapsid ring whose diameter, cavity, and pitch/height dimensions agree with EM data from early studies on the Paramyxovirinae subfamily of native RNPs, indicating that it closely represents one-turn in the building block of the RNP helices. The PIV5-N nucleocapsid ring encapsidates a nuclease resistant 78-nt RNA strand in its positively charged groove formed between the N-terminal (NTD) and C-terminal (CTD) domains of its successive N protomers. Six nucleotides precisely are associated with each N protomer, with alternating three-base-in three-base-out conformation. The binding of six nucleotides per protomer is consistent with the “rule of six” that governs the genome packaging of the Paramyxovirinae subfamily of viruses. PIV5-N protomer subdomains are very similar in structure to the previously solved Nipah-N structure, but with a difference in the angle between NTD/CTD at the RNA hinge region. Based on the Nipah-N structure we modeled a PIV5-N open conformation in which the CTD rotates away from the RNA strand into the inner spacious nucleocapsid-ring cavity. Finally, this rotation would expose the RNA for the viral polymerase activity without major disruption of the nucleocapsid structure.
Report Numbers
E 1.99:1182328
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Note
Published through SciTech Connect.
03/23/2015.
Proceedings of the National Academy of Sciences of the United States of America 112 14 ISSN 0027-8424 AM
Maher Alayyoubi; George P. Leser; Christopher A. Kors; Robert A. Lamb.
Northwestern Univ., Evanston, IL (United States)
Michigan Economic Development Corporation (United States)
Michigan Technology Tri-Corridor (United States)
Funding Information
AC02-06CH11357
085PI000817
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