1mwh: Difference between revisions
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==REOVIRUS POLYMERASE LAMBDA3 BOUND TO MRNA CAP ANALOG== | ==REOVIRUS POLYMERASE LAMBDA3 BOUND TO MRNA CAP ANALOG== | ||
<StructureSection load='1mwh' size='340' side='right' caption='[[1mwh]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='1mwh' size='340' side='right' caption='[[1mwh]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1muk|1muk]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1muk|1muk]]</td></tr> | ||
<tr id='gene'><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])</td></tr> | <tr id='gene'><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])</td></tr> | ||
<tr id='resources'><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://pdbe.org/1mwh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mwh RCSB], [http://www.ebi.ac.uk/pdbsum/1mwh PDBsum]</span></td></tr> | <tr id='resources'><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://pdbe.org/1mwh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mwh RCSB], [http://www.ebi.ac.uk/pdbsum/1mwh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mwh ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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Revision as of 13:13, 25 October 2017
REOVIRUS POLYMERASE LAMBDA3 BOUND TO MRNA CAP ANALOGREOVIRUS POLYMERASE LAMBDA3 BOUND TO MRNA CAP ANALOG
Structural highlights
Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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