1n1h

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(New page: 200px<br /><applet load="1n1h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n1h, resolution 2.80&Aring;" /> '''Initiation complex o...)
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[[Image:1n1h.gif|left|200px]]<br /><applet load="1n1h" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1n1h.gif|left|200px]]<br /><applet load="1n1h" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1n1h, resolution 2.80&Aring;" />
caption="1n1h, resolution 2.80&Aring;" />
'''Initiation complex of polymerase lambda3 from reovirus'''<br />
'''Initiation complex of polymerase lambda3 from reovirus'''<br />
==Overview==
==Overview==
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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.
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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==
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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 MN, G7M, GDP, CH1 and GH3 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1N1H OCA].
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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].
==Reference==
==Reference==
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[[Category: Mammalian orthoreovirus 3]]
[[Category: Mammalian orthoreovirus 3]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Farsetta, D.L.]]
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[[Category: Farsetta, D L.]]
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[[Category: Harrison, S.C.]]
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[[Category: Harrison, S C.]]
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[[Category: Nibert, M.L.]]
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[[Category: Nibert, M L.]]
[[Category: Tao, Y.]]
[[Category: Tao, Y.]]
[[Category: CH1]]
[[Category: CH1]]
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[[Category: right hand configuration]]
[[Category: right hand configuration]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:52:22 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:01:15 2008''

Revision as of 12:01, 21 February 2008


1n1h, resolution 2.80Å

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Initiation complex of polymerase lambda3 from reovirus

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

1N1H is a Single protein structure of sequence from Mammalian orthoreovirus 3 with , , , and 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

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