1u09: Difference between revisions
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'''Footand Mouth Disease Virus RNA-dependent RNA polymerase''' | '''Footand Mouth Disease Virus RNA-dependent RNA polymerase''' | ||
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==About this Structure== | ==About this Structure== | ||
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U09 OCA]. | |||
==Reference== | ==Reference== | ||
Structure of foot-and-mouth disease virus RNA-dependent RNA polymerase and its complex with a template-primer RNA., Ferrer-Orta C, Arias A, Perez-Luque R, Escarmis C, Domingo E, Verdaguer N, J Biol Chem. 2004 Nov 5;279(45):47212-21. Epub 2004 Aug 3. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15294895 15294895] | Structure of foot-and-mouth disease virus RNA-dependent RNA polymerase and its complex with a template-primer RNA., Ferrer-Orta C, Arias A, Perez-Luque R, Escarmis C, Domingo E, Verdaguer N, J Biol Chem. 2004 Nov 5;279(45):47212-21. Epub 2004 Aug 3. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15294895 15294895] | ||
[[Category: RNA-directed RNA polymerase]] | [[Category: RNA-directed RNA polymerase]] | ||
[[Category: Arias, A.]] | [[Category: Arias, A.]] | ||
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[[Category: Perez-Luque, R.]] | [[Category: Perez-Luque, R.]] | ||
[[Category: Verdaguer, N.]] | [[Category: Verdaguer, N.]] | ||
[[Category: | [[Category: Foot and mouth disease virus]] | ||
[[Category: | [[Category: Protein-dna complex]] | ||
[[Category: | [[Category: Rna-dependent rna polymerase]] | ||
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Revision as of 10:35, 3 May 2008
Footand Mouth Disease Virus RNA-dependent RNA polymerase
OverviewOverview
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.
About this StructureAbout this Structure
Full crystallographic information is available from OCA.
ReferenceReference
Structure of foot-and-mouth disease virus RNA-dependent RNA polymerase and its complex with a template-primer RNA., Ferrer-Orta C, Arias A, Perez-Luque R, Escarmis C, Domingo E, Verdaguer N, J Biol Chem. 2004 Nov 5;279(45):47212-21. Epub 2004 Aug 3. PMID:15294895 Page seeded by OCA on Sat May 3 10:35:18 2008