1WNE

Foot and Mouth Disease Virus RNA-dependent RNA polymerase in complex with a template-primer RNA

Summary for 1WNE

• Entry DOI: 10.2210/pdb1wne/pdb
• Related: 1U09
• Descriptor: 5'-R(*CP*AP*UP*GP*GP*GP*CP*C)-3', 5'-R(*GP*GP*CP*CP*C)-3', RNA-dependent RNA polymerase, ... (5 entities in total)
• Functional Keywords: protein-dna complex, foot and mouth disease virus, rna-dependent rna polymerase, transferase-rna complex, transferase/rna
• Biological source: Foot-and-mouth disease virus
• Cellular location: Picornain 3C: Host cytoplasm (By similarity): Q9QCE4
• Total number of polymer chains: 3
• Total formula weight: 57613.57

Authors

Ferrer-Orta, C.,Arias, A.,Perez-Luque, R.,Escarmis, C.,Domingo, E.,Verdaguer, N. (deposition date: 2004-07-31, release date: 2004-08-31, Last modification date: 2023-10-25)

Primary citation

Ferrer-Orta, C.,Arias, A.,Perez-Luque, R.,Escarmis, C.,Domingo, E.,Verdaguer, N.
Structure of Foot-and-Mouth Disease Virus RNA-dependent RNA Polymerase and Its Complex with a Template-Primer RNA
J.Biol.Chem., 279:47212-47221, 2004

PubMed Abstract: 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.

PubMed: 15294895
DOI: 10.1074/jbc.M405465200

Experimental method

X-RAY DIFFRACTION (3 Å)