1n38: Difference between revisions

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New page: left|200px<br /><applet load="1n38" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n38, resolution 2.8Å" /> '''reovirus polymerase l...
 
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[[Image:1n38.gif|left|200px]]<br /><applet load="1n38" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1n38.gif|left|200px]]<br /><applet load="1n38" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1n38, resolution 2.8&Aring;" />
caption="1n38, resolution 2.8&Aring;" />
'''reovirus polymerase lambda3 elongation complex with one phosphodiester bond formed'''<br />
'''reovirus polymerase lambda3 elongation complex with one phosphodiester bond formed'''<br />


==Overview==
==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.
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==
==About this Structure==
1N38 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 MN, U3H and CH1 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1N38 OCA].  
1N38 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=U3H:'>U3H</scene> and <scene name='pdbligand=CH1:'>CH1</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N38 OCA].  


==Reference==
==Reference==
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[[Category: Mammalian orthoreovirus 3]]
[[Category: Mammalian orthoreovirus 3]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Farsetta, D.L.]]
[[Category: Farsetta, D L.]]
[[Category: Harrison, S.C.]]
[[Category: Harrison, S C.]]
[[Category: Nibert, M.L.]]
[[Category: Nibert, M L.]]
[[Category: Tao, Y.]]
[[Category: Tao, Y.]]
[[Category: CH1]]
[[Category: CH1]]
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[[Category: rna polymerase]]
[[Category: rna polymerase]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:55:35 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:01:45 2008''