2ckw
From Proteopedia
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'''THE 2.3 A RESOLUTION STRUCTURE OF THE SAPPORO VIRUS RNA DEPENDANT RNA POLYMERASE.''' | '''THE 2.3 A RESOLUTION STRUCTURE OF THE SAPPORO VIRUS RNA DEPENDANT RNA POLYMERASE.''' | ||
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[[Category: Rohayem, J.]] | [[Category: Rohayem, J.]] | ||
[[Category: Tucker, P A.]] | [[Category: Tucker, P A.]] | ||
| - | [[Category: | + | [[Category: Atp-binding]] |
| - | [[Category: | + | [[Category: Capsid protein]] |
| - | [[Category: | + | [[Category: Covalent protein-rna linkage]] |
| - | [[Category: | + | [[Category: Helicase]] |
| - | [[Category: | + | [[Category: Hydrolase]] |
| - | [[Category: | + | [[Category: Mutant]] |
| - | [[Category: | + | [[Category: Nucleotide-binding]] |
| - | [[Category: | + | [[Category: Nucleotidyltransferase]] |
| - | [[Category: | + | [[Category: Polymerase]] |
| - | [[Category: | + | [[Category: Polyprotein]] |
| - | [[Category: | + | [[Category: Protease]] |
| - | [[Category: | + | [[Category: Rna elongation]] |
| - | [[Category: | + | [[Category: Rna replication]] |
| - | [[Category: | + | [[Category: Rna-directed rna polymerase]] |
| - | [[Category: | + | [[Category: Structural protein]] |
| - | [[Category: | + | [[Category: Thiol protease]] |
| - | [[Category: | + | [[Category: Transferase]] |
| - | [[Category: | + | [[Category: Transferase activity]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 22:23:08 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 19:23, 3 May 2008
THE 2.3 A RESOLUTION STRUCTURE OF THE SAPPORO VIRUS RNA DEPENDANT RNA POLYMERASE.
Overview
Sapoviruses are one of the major agents of acute gastroenteritis in childhood. They form a tight genetic cluster (genus) in the Caliciviridae family that regroups both animal and human pathogenic strains. No permissive tissue culture has been developed for human sapovirus, limiting its characterization to surrogate systems. We report here on the first extensive characterization of the key enzyme of replication, the RNA-dependent RNA polymerase (RdRp) associated with the 3D(pol)-like protein. Enzymatically active sapovirus 3D(pol) and its defective mutant were expressed in Escherichia coli and purified. The overall structure of the sapovirus 3D(pol) was determined by X-ray crystallography to 2.32-A resolution. It revealed a right hand fold typical for template-dependent polynucleotide polymerases. The carboxyl terminus is located within the active site cleft, as observed in the RdRp of some (norovirus) but not other (lagovirus) caliciviruses. Sapovirus 3D(pol) prefers Mn(2+) over Mg(2+) but may utilize either as a cofactor in vitro. In a synthetic RNA template-dependent reaction, sapovirus 3D(pol) synthesizes a double-stranded RNA or labels the template 3' terminus by terminal transferase activity. Initiation of RNA synthesis occurs de novo on heteropolymeric templates or in a primer-dependent manner on polyadenylated templates. Strikingly, this mode of initiation of RNA synthesis was also described for norovirus, but not for lagovirus, suggesting structural and functional homologies in the RNA-dependent RNA polymerase of human pathogenic caliciviruses. This first experimental evidence makes sapovirus 3D(pol) an attractive target for developing drugs to control calicivirus infection in humans.
About this Structure
2CKW is a Single protein structure of sequence from Sapporo virus. Full crystallographic information is available from OCA.
Reference
Structural and functional characterization of sapovirus RNA-dependent RNA polymerase., Fullerton SW, Blaschke M, Coutard B, Gebhardt J, Gorbalenya A, Canard B, Tucker PA, Rohayem J, J Virol. 2007 Feb;81(4):1858-71. Epub 2006 Nov 22. PMID:17121797 Page seeded by OCA on Sat May 3 22:23:08 2008
Categories: RNA-directed RNA polymerase | Sapporo virus | Single protein | Canard, B. | Coutard, B. | Fullerton, S W.B. | Gebhardt, J. | Gorbalenya, A. | Rohayem, J. | Tucker, P A. | Atp-binding | Capsid protein | Covalent protein-rna linkage | Helicase | Hydrolase | Mutant | Nucleotide-binding | Nucleotidyltransferase | Polymerase | Polyprotein | Protease | Rna elongation | Rna replication | Rna-directed rna polymerase | Structural protein | Thiol protease | Transferase | Transferase activity
