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'''reovirus lambda3 native structure''' | '''reovirus lambda3 native structure''' | ||
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[[Category: Nibert, M L.]] | [[Category: Nibert, M L.]] | ||
[[Category: Tao, Y.]] | [[Category: Tao, Y.]] | ||
[[Category: | [[Category: Finger]] | ||
[[Category: | [[Category: Palm]] | ||
[[Category: | [[Category: Right hand configuration]] | ||
[[Category: | [[Category: Single subunit polymerase fold]] | ||
[[Category: | [[Category: Thumb]] | ||
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Revision as of 22:44, 2 May 2008
reovirus lambda3 native structure
Overview
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 Structure
1MUK is a Single protein structure of sequence from Reovirus sp.. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Sat May 3 01:44:21 2008
