1mwh
From Proteopedia
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| - | [[ | + | ==REOVIRUS POLYMERASE LAMBDA3 BOUND TO MRNA CAP ANALOG== |
| + | <StructureSection load='1mwh' size='340' side='right' caption='[[1mwh]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1mwh]] is a 1 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MWH FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GTG:7-METHYL-GUANOSINE-5-TRIPHOSPHATE-5-GUANOSINE'>GTG</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1muk|1muk]]</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">L1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10891 Reovirus sp.])</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1mwh RCSB], [http://www.ebi.ac.uk/pdbsum/1mwh PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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<ref>PMID:12464184</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
| - | == | + | |
| - | < | + | |
[[Category: Reovirus sp.]] | [[Category: Reovirus sp.]] | ||
[[Category: Farsetta, D L.]] | [[Category: Farsetta, D L.]] | ||
Revision as of 18:26, 28 September 2014
REOVIRUS POLYMERASE LAMBDA3 BOUND TO MRNA CAP ANALOG
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