1mwh: Difference between revisions
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|PDB= 1mwh |SIZE=350|CAPTION= <scene name='initialview01'>1mwh</scene>, resolution 2.50Å | |PDB= 1mwh |SIZE=350|CAPTION= <scene name='initialview01'>1mwh</scene>, resolution 2.50Å | ||
|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= <scene name='pdbligand=GTG:7-METHYL-GUANOSINE-5'-TRIPHOSPHATE-5'-GUANOSINE'>GTG</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= L1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10891 Reovirus sp.]) | |GENE= L1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10891 Reovirus sp.]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1muk|1MUK]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mwh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mwh OCA], [http://www.ebi.ac.uk/pdbsum/1mwh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mwh RCSB]</span> | |||
}} | }} | ||
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[[Category: Nibert, M L.]] | [[Category: Nibert, M L.]] | ||
[[Category: Tao, Y.]] | [[Category: Tao, Y.]] | ||
[[Category: polymerase]] | [[Category: polymerase]] | ||
[[Category: polymerase-cap analog complex]] | [[Category: polymerase-cap analog complex]] | ||
[[Category: right hand configuration]] | [[Category: right hand configuration]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:22:06 2008'' |
Revision as of 22:22, 30 March 2008
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, resolution 2.50Å | |||||||
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Ligands: | , | ||||||
Gene: | L1 (Reovirus sp.) | ||||||
Related: | 1MUK
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Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
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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