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RNA synthesis in a cage--structural studies of reovirus polymerase lambda3.

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.[1]

References

  1. RNA synthesis in a cage--structural studies of reovirus polymerase lambda3. Tao, Y., Farsetta, D.L., Nibert, M.L., Harrison, S.C. Cell (2002) [Pubmed]
 
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