1mwh
From Proteopedia
(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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| - | [[Image:1mwh.jpg|left|200px]]<br /><applet load="1mwh" size=" | + | [[Image:1mwh.jpg|left|200px]]<br /><applet load="1mwh" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1mwh, resolution 2.50Å" /> | caption="1mwh, resolution 2.50Å" /> | ||
'''REOVIRUS POLYMERASE LAMBDA3 BOUND TO MRNA CAP ANALOG'''<br /> | '''REOVIRUS POLYMERASE LAMBDA3 BOUND TO MRNA CAP ANALOG'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The reovirus polymerase and those of other dsRNA viruses function within | + | 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== | ||
| - | 1MWH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Reovirus_sp. Reovirus sp.] with MN and GTG as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1MWH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Reovirus_sp. Reovirus sp.] with <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=GTG:'>GTG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MWH OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Reovirus sp.]] | [[Category: Reovirus sp.]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Farsetta, D | + | [[Category: Farsetta, D L.]] |
| - | [[Category: Harrison, S | + | [[Category: Harrison, S C.]] |
| - | [[Category: Nibert, M | + | [[Category: Nibert, M L.]] |
[[Category: Tao, Y.]] | [[Category: Tao, Y.]] | ||
[[Category: GTG]] | [[Category: GTG]] | ||
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[[Category: right hand configuration]] | [[Category: right hand configuration]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:59:44 2008'' |
Revision as of 11:59, 21 February 2008
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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 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
Page seeded by OCA on Thu Feb 21 13:59:44 2008
