Structure of foot-and-mouth disease virus RNA-dependent RNA polymerase and its complex with a template-primer RNA.
Genome 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.
Ferrer-Orta
Cristina
C
Institut de Biologia Molecular de Barcelona (CSIC), Parc Científic de Barcelona, Josep Samitier 1-5, E-08028 Barcelona, Spain.
Arias
Armando
A
Perez-Luque
Rosa
R
Escarmís
Cristina
C
Domingo
Esteban
E
Verdaguer
Nuria
N
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D001665:Binding Sites; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray; D004583:Electrons; D029544:Foot-and-Mouth Disease Virus / Q000201:enzymology* / Q000235:genetics*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010957:Plasmids / Q000378:metabolism; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012313:RNA / Q000737:chemistry; D012367:RNA, Viral; D012324:RNA-Dependent RNA Polymerase / Q000737:chemistry*; D011994:Recombinant Proteins / Q000737:chemistry; D017386:Sequence Homology, Amino Acid
D012367:RNA, Viral; D011994:Recombinant Proteins; D012313:RNA; D012324:RNA-Dependent RNA Polymerase