1n1h: Difference between revisions

[[Image:1n1h.gif|left|200px]]<br /><applet load="1n1h" size="350" color="white" frame="true" align="right" spinBox="true"  

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.

1N1H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mammalian_orthoreovirus_3 Mammalian orthoreovirus 3] with <scene name='pdbligand=MN:'>MN</scene>, <scene name='pdbligand=G7M:'>G7M</scene>, <scene name='pdbligand=GDP:'>GDP</scene>, <scene name='pdbligand=CH1:'>CH1</scene> and <scene name='pdbligand=GH3:'>GH3</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N1H OCA].  

[[Category: Farsetta, D L.]]

[[Category: Harrison, S C.]]

[[Category: Nibert, M L.]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:01:15 2008''