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Structure of foot-and-mouth disease virus RNA-dependent RNA polymerase and its complex with a template-primer RNA

AutorFerrer-Orta, Cristina ; Arias, Armando ; Pérez-Luque, Rosa ; Escarmís, Cristina; Domingo, Esteban ; Verdaguer, Núria
Fecha de publicación5-nov-2004
EditorAmerican Society for Biochemistry and Molecular Biology
CitaciónJournal of Biological Chemistry 279(45): 47212-47221 (2004)
ResumenGenome replication in picornaviruses is catalyzed by a virally encoded RNA-dependent RNA polymerase, termed 3D. The enzyme performs this operation, together with other viral and probably host proteins, in the cytoplasm of their host cells. The crystal structure of the 3D polymerase of foot-and-mouth disease virus, one of the most important animal pathogens, has been determined unliganded and bound to a template-primer RNA decanucleotide. The enzyme folds in the characteristic fingers, palm and thumb subdomains, with the presence of an NH2-terminal segment that encircles the active site. In the complex, several conserved amino acid side chains bind to the template-primer, likely mediating the initiation of RNA synthesis. The structure provides essential information for studies on RNA replication and the design of antiviral compounds.
Versión del editorhttp://dx.doi.org/10.1074/jbc.M405465200
URIhttp://hdl.handle.net/10261/110047
DOI10.1074/jbc.M405465200
Identificadoresdoi: 10.1074/jbc.M405465200
issn: 0021-9258
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