1mwh: Difference between revisions
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[[Image:1mwh.jpg|left|200px]] | [[Image:1mwh.jpg|left|200px]] | ||
'''REOVIRUS POLYMERASE LAMBDA3 BOUND TO MRNA CAP ANALOG''' | {{Structure | ||
|PDB= 1mwh |SIZE=350|CAPTION= <scene name='initialview01'>1mwh</scene>, resolution 2.50Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> and <scene name='pdbligand=GTG:7-METHYL-GUANOSINE-5'-TRIPHOSPHATE-5'-GUANOSINE'>GTG</scene> | |||
|ACTIVITY= | |||
|GENE= L1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10891 Reovirus sp.]) | |||
}} | |||
'''REOVIRUS POLYMERASE LAMBDA3 BOUND TO MRNA CAP ANALOG''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1MWH is a [ | 1MWH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Reovirus_sp. Reovirus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MWH OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12464184 12464184] | ||
[[Category: Reovirus sp.]] | [[Category: Reovirus sp.]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: right hand configuration]] | [[Category: right hand configuration]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:49:06 2008'' |
Revision as of 13:49, 20 March 2008
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, resolution 2.50Å | |||||||
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Ligands: | and | ||||||
Gene: | L1 (Reovirus sp.) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
REOVIRUS POLYMERASE LAMBDA3 BOUND TO MRNA CAP ANALOG
OverviewOverview
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 StructureAbout this Structure
1MWH is a Single protein structure of sequence from Reovirus sp.. Full crystallographic information is available from OCA.
ReferenceReference
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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