1mwh
REOVIRUS POLYMERASE LAMBDA3 BOUND TO MRNA CAP ANALOG
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| , resolution 2.50Å | |||||||
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| Ligands: | and | ||||||
| Gene: | L1 (Reovirus sp.) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
OverviewOverview
The reovirus polymerase and those of other dsRNA viruses function within the confines of a protein capsid to transcribe the tightly packed dsRNA genome segments. The crystal structure of the reovirus polymerase, lambda3, determined at 2.5 A resolution, shows a fingers-palm-thumb core, similar to those of other viral polymerases, surrounded by major N- and C-terminal elaborations, which create a cage-like structure, with four channels leading to the catalytic site. This "caged" polymerase has allowed us to visualize the results of several rounds of RNA polymerization directly in the crystals. A 5' cap binding site on the surface of lambda3 suggests a template retention mechanism by which attachment of the 5' end of the plus-sense strand facilitates insertion of the 3' end of the minus-sense strand into the template channel.
About this StructureAbout this Structure
1MWH is a Single protein structure of sequence from Reovirus sp.. Full crystallographic information is available from OCA.
ReferenceReference
RNA synthesis in a cage--structural studies of reovirus polymerase lambda3., Tao Y, Farsetta DL, Nibert ML, Harrison SC, Cell. 2002 Nov 27;111(5):733-45. PMID:12464184
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