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3avv
From Proteopedia
(Difference between revisions)
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| - | + | ==Structure of viral RNA polymerase complex 3== | |
| - | + | <StructureSection load='3avv' size='340' side='right' caption='[[3avv]], [[Resolution|resolution]] 3.12Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[3avv]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_o157:h7 Escherichia coli o157:h7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AVV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3AVV FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3avt|3avt]], [[3avu|3avu]], [[3avw|3avw]], [[3avx|3avx]], [[3avy|3avy]]</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=3avv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3avv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3avv RCSB], [http://www.ebi.ac.uk/pdbsum/3avv PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Core Qbeta replicase comprises the Qbeta virus-encoded RNA-dependent RNA polymerase (beta-subunit) and the host Escherichia coli translational elongation factors EF-Tu and EF-Ts. The functions of the host proteins in the viral replicase are not clear. Structural analyses of RNA polymerization by core Qbeta replicase reveal that at the initiation stage, the 3'-adenine of the template RNA provides a stable platform for de novo initiation. EF-Tu in Qbeta replicase forms a template exit channel with the beta-subunit. At the elongation stages, the C-terminal region of the beta-subunit, assisted by EF-Tu, splits the temporarily double-stranded RNA between the template and nascent RNAs before translocation of the single-stranded template RNA into the exit channel. Therefore, EF-Tu in Qbeta replicase modulates RNA elongation processes in a distinct manner from its established function in protein synthesis. | ||
| - | + | Molecular basis for RNA polymerization by Qbeta replicase.,Takeshita D, Tomita K Nat Struct Mol Biol. 2012 Jan 15;19(2):229-37. doi: 10.1038/nsmb.2204. PMID:22245970<ref>PMID:22245970</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | == | + | <references/> |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
[[Category: Escherichia coli o157:h7]] | [[Category: Escherichia coli o157:h7]] | ||
| - | [[Category: Takeshita, D | + | [[Category: Takeshita, D]] |
| - | [[Category: Tomita, K | + | [[Category: Tomita, K]] |
[[Category: Rna polymerase]] | [[Category: Rna polymerase]] | ||
[[Category: Transferase-rna complex]] | [[Category: Transferase-rna complex]] | ||
[[Category: Translation]] | [[Category: Translation]] | ||
Revision as of 13:13, 18 December 2014
Structure of viral RNA polymerase complex 3
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