1mwh
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(New page: 200px<br /><applet load="1mwh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mwh, resolution 2.50Å" /> '''REOVIRUS POLYMERASE ...)
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Revision as of 19:38, 20 November 2007
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REOVIRUS POLYMERASE LAMBDA3 BOUND TO MRNA CAP ANALOG
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
1MWH is a Single protein structure of sequence from Reovirus sp. with MN and GTG as ligands. 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 Tue Nov 20 21:45:50 2007
