{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Fernandez-Garcia Y"],"funding":["Comisión Nacional de Investigación Científica y Tecnológica","Deutsche Forschungsgemeinschaft"],"pagination":["e1005635"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4907427"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["12(6)"],"pubmed_abstract":["Andes virus (ANDV) is a human-pathogenic hantavirus. Hantaviruses presumably initiate their mRNA synthesis by using cap structures derived from host cell mRNAs, a mechanism called cap-snatching. A signature for a cap-snatching endonuclease is present in the N terminus of hantavirus L proteins. In this study, we aimed to solve the atomic structure of the ANDV endonuclease and characterize its biochemical features. However, the wild-type protein was refractory to expression in Escherichia coli, presumably due to toxic enzyme activity. To circumvent this problem, we introduced attenuating mutations in the domain that were previously shown to enhance L protein expression in mammalian cells. Using this approach, 13 mutant proteins encompassing ANDV L protein residues 1-200 were successfully exp"],"journal":["PLoS pathogens"],"pubmed_title":["Atomic Structure and Biochemical Characterization of an RNA Endonuclease in the N Terminus of Andes Virus L Protein."],"pmcid":["PMC4907427"],"funding_grant_id":["21110444 and BCH2014-7571","RE 3712/1-1"],"pubmed_authors":["Cusack S","Reguera J","Fernandez-Garcia Y","Sanchez-Ramos O","Betzel C","Witte G","Gunther S","Reindl S","Busch C"],"additional_accession":[]},"is_claimable":false,"name":"Atomic Structure and Biochemical Characterization of an RNA Endonuclease in the N Terminus of Andes Virus L Protein.","description":"Andes virus (ANDV) is a human-pathogenic hantavirus. Hantaviruses presumably initiate their mRNA synthesis by using cap structures derived from host cell mRNAs, a mechanism called cap-snatching. A signature for a cap-snatching endonuclease is present in the N terminus of hantavirus L proteins. In this study, we aimed to solve the atomic structure of the ANDV endonuclease and characterize its biochemical features. However, the wild-type protein was refractory to expression in Escherichia coli, presumably due to toxic enzyme activity. To circumvent this problem, we introduced attenuating mutations in the domain that were previously shown to enhance L protein expression in mammalian cells. Using this approach, 13 mutant proteins encompassing ANDV L protein residues 1-200 were successfully exp","dates":{"release":"2016-01-01T00:00:00Z","publication":"2016 Jun","modification":"2026-05-30T12:43:10.927Z","creation":"2019-03-26T22:50:47Z"},"accession":"S-EPMC4907427","cross_references":{"pubmed":["27300328"],"doi":["10.1371/journal.ppat.1005635"]}}