1u09

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1u09" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u09, resolution 1.91&Aring;" /> '''Footand Mouth Diseas...)
Line 1: Line 1:
-
[[Image:1u09.gif|left|200px]]<br /><applet load="1u09" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1u09.gif|left|200px]]<br /><applet load="1u09" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1u09, resolution 1.91&Aring;" />
caption="1u09, resolution 1.91&Aring;" />
'''Footand Mouth Disease Virus RNA-dependent RNA polymerase'''<br />
'''Footand Mouth Disease Virus RNA-dependent RNA polymerase'''<br />
==Overview==
==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.
+
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==
-
1U09 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]. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1U09 OCA].
+
1U09 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]. 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=1U09 OCA].
==Reference==
==Reference==
Line 24: Line 24:
[[Category: rna-dependent rna polymerase]]
[[Category: rna-dependent rna polymerase]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 03:04:32 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:19:13 2008''

Revision as of 13:19, 21 February 2008


1u09, resolution 1.91Å

Drag the structure with the mouse to rotate

Footand Mouth Disease Virus RNA-dependent RNA polymerase

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

1U09 is a Protein complex structure of sequences from Foot-and-mouth disease virus. 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

Page seeded by OCA on Thu Feb 21 15:19:13 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools