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3T5N

1.8A crystal structure of Lassa virus nucleoprotein in complex with ssRNA

Summary for 3T5N
Entry DOI10.2210/pdb3t5n/pdb
Related3T5Q
DescriptorNucleoprotein, RNA (5'-R(P*UP*AP*UP*CP*UP*C)-3'), NICKEL (II) ION, ... (4 entities in total)
Functional Keywordsssrna, single stranded rna, viral protein-rna complex, viral protein/rna
Biological sourceMopeia Lassa reassortant 29
More
Cellular locationVirion: Q5S585
Total number of polymer chains2
Total formula weight41212.36
Authors
Hastie, K.M.,Liu, T.,King, L.B.,Ngo, N.,Zandonatti, M.A.,Woods, V.L.,de la Torre, J.C.,Saphire, E.O. (deposition date: 2011-07-27, release date: 2012-01-11, Last modification date: 2024-02-28)
Primary citationHastie, K.M.,Liu, T.,Li, S.,King, L.B.,Ngo, N.,Zandonatti, M.A.,Woods, V.L.,de la Torre, J.C.,Saphire, E.O.
Crystal structure of the Lassa virus nucleoprotein-RNA complex reveals a gating mechanism for RNA binding.
Proc.Natl.Acad.Sci.USA, 108:19365-19370, 2011
Cited by
PubMed Abstract: Arenaviruses cause disease in industrialized and developing nations alike. Among them, the hemorrhagic fever virus Lassa is responsible for ~300,000-500,000 infections/y in Western Africa. The arenavirus nucleoprotein (NP) forms the protein scaffold of the genomic ribonucleoprotein complexes and is critical for transcription and replication of the viral genome. Here, we present crystal structures of the RNA-binding domain of Lassa virus NP in complex with ssRNA. This structure shows, in contrast to the predicted model, that RNA binds in a deep, basic crevice located entirely within the N-terminal domain. Furthermore, the NP-ssRNA structures presented here, combined with hydrogen-deuterium exchange/MS and functional studies, suggest a gating mechanism by which NP opens to accept RNA. Directed mutagenesis and functional studies provide a unique look into how the arenavirus NPs bind to and protect the viral genome and also suggest the likely assembly by which viral ribonucleoprotein complexes are organized.
PubMed: 22084115
DOI: 10.1073/pnas.1108515108
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.787 Å)
Structure validation

226707

数据于2024-10-30公开中

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