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dc.contributor.otherUniversidad San Pablo-CEU. Facultad de Farmacia-
dc.contributor.otherGrupo: Parasitología e Inmunología molecular con aplicación biotecnológica, diagnóstica y terapéutica (PARINM)-
dc.creatorFerrer-Orta, Cristina-
dc.creatorArias, Armando-
dc.creatorAgudo Torres, Rubén-
dc.creatorPérez-Luque, Rosa-
dc.creatorEscarmís, Cristina-
dc.creatorDomingo, Esteban-
dc.creatorVerdaguer, Nuria-
dc.date.accessioned2024-03-21T14:39:09Z-
dc.date.available2024-03-21T14:39:09Z-
dc.date.issued2006-02-02-
dc.identifier.citationThe structure of a protein primer-polymerase complex in the initiation of genoma replication. Ferrer-Orta C, Arias A, Agudo R, Pérez-Luque R, Escarmís C, Domingo A, Verdaguer N. EMBO Journal. 25(4), pp. 880 - 888 (2006).en_EN
dc.identifier.issn1460-2075-
dc.identifier.urihttp://hdl.handle.net/10637/15657-
dc.description.abstractPicornavirus RNA replication is initiated by the covalent attachment of a UMP molecule to the hydroxyl group of a tyrosine in the terminal protein VPg. This reaction is carried out by the viral RNA-dependent RNA polymerase (3D). Here, we report the X-ray structure of two complexes between foot-and-mouth disease virus 3D, VPg1, the substrate UTP and divalent cations, in the absence and in the presence of an oligoadenylate of 10 residues. In both complexes, VPg fits the RNA binding cleft of the polymerase and projects the key residue Tyr3 into the active site of 3D. This is achieved by multiple interactions with residues of motif F and helix a8 of the fingers domain and helix a13 of the thumb domain of the polymerase. The complex obtained in the presence of the oligoadenylate showed the product of the VPg uridylylation (VPg-UMP). Two metal ions and the catalytic aspartic acids of the polymerase active site, together with the basic residues of motif F, have been identified as participating in the priming reaction.en_EN
dc.language.isoen-
dc.publisherEMBO Pressen_EN
dc.relation.ispartofThe EMBO Journal-
dc.rightshttp://creativecommons.org/licenses/by-nc-nd/4.0/deed.es-
dc.subjectFoot-and-mouth disease virusen_EN
dc.subjectPrimer–proteinen_EN
dc.subjectReplicationen_EN
dc.subjectUridylylationen_EN
dc.subjectVPgen_EN
dc.titleThe structure of a protein primer–polymerase complex in the initiation of genome replicationen_EN
dc.typeArtículoen_EN
dc.identifier.doi10.1038/ sj.emboj.7600971-
dc.relation.projectIDGrants BIO2002-00517 and BFU2005-02376/BMC. Work in Madrid by Grants BMC 2001.1823.C02-01, BFU2005-00863/BMC and Fundacio´n R Areces. CF and AA were supported by I3P fellowships from Ministerio de Educacio´n y Ciencia. RA was supported by an FPI fellowship from Comunidad de Madrid. Data were collected at the EMBL protein crystallography beam lines ID14.2, ID14.4 and BM16 at ESRF (Grenoble) within a Block Allocation Group (BAG Barcelona). The financial support was provided by the ESRF.-
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