1wne
From Proteopedia
(New page: 200px<br /><applet load="1wne" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wne, resolution 3.00Å" /> '''Foot and Mouth Disea...) |
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| - | [[Image:1wne.gif|left|200px]]<br /><applet load="1wne" size=" | + | [[Image:1wne.gif|left|200px]]<br /><applet load="1wne" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1wne, resolution 3.00Å" /> | caption="1wne, resolution 3.00Å" /> | ||
'''Foot and Mouth Disease Virus RNA-dependent RNA polymerase in complex with a template-primer RNA'''<br /> | '''Foot and Mouth Disease Virus RNA-dependent RNA polymerase in complex with a template-primer RNA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Genome replication in picornaviruses is catalyzed by a virally encoded | + | 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 Structure== | ==About this Structure== | ||
| - | 1WNE is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Foot_and_mouth_disease_virus Foot and mouth disease virus] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/RNA-directed_RNA_polymerase RNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.48 2.7.7.48] Full crystallographic information is available from [http:// | + | 1WNE is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Foot_and_mouth_disease_virus Foot and mouth disease virus] with <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/RNA-directed_RNA_polymerase RNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.48 2.7.7.48] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WNE OCA]. |
==Reference== | ==Reference== | ||
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[[Category: rna-dependent rna polymerase]] | [[Category: rna-dependent rna polymerase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:46:11 2008'' |
Revision as of 13:46, 21 February 2008
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Foot and Mouth Disease Virus RNA-dependent RNA polymerase in complex with a template-primer RNA
Overview
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 Structure
1WNE is a Protein complex structure of sequences from Foot and mouth disease virus with as ligand. Active as RNA-directed RNA polymerase, with EC number 2.7.7.48 Full crystallographic information is available from OCA.
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:15294895
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