View source for 3vnu


==Complex structure of viral RNA polymerase I==
<StructureSection load='3vnu' size='340' side='right'caption='[[3vnu]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3vnu]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7] and [https://en.wikipedia.org/wiki/Escherichia_virus_Qbeta Escherichia virus Qbeta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VNU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VNU FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3vnu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vnu OCA], [https://pdbe.org/3vnu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vnu RCSB], [https://www.ebi.ac.uk/pdbsum/3vnu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vnu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/EFTU_ECO57 EFTU_ECO57] [https://www.uniprot.org/uniprot/EFTS_ECO57 EFTS_ECO57] Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome (By similarity).[https://www.uniprot.org/uniprot/RDRP_BPQBE RDRP_BPQBE] This enzyme is part of the viral RNA-dependent RNA polymerase complex.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The genomic RNA of Qbeta virus is replicated by Qbeta replicase, a template-dependent RNA polymerase complex. Qbeta replicase has an intrinsic template-independent RNA 3'-adenylation activity, which is required for efficient viral RNA amplification in the host cells. However, the mechanism of the template-independent 3'-adenylation of RNAs by Qbeta replicase has remained elusive. We determined the structure of a complex that includes Qbeta replicase, a template RNA, a growing RNA complementary to the template RNA, and ATP. The structure represents the terminal stage of RNA polymerization and reveals that the shape and size of the nucleotide-binding pocket becomes available for ATP accommodation after the 3'-penultimate template-dependent C-addition. The stacking interaction between the ATP and the neighboring Watson-Crick base pair, between the 5'-G in the template and the 3'-C in the growing RNA, contributes to the nucleotide specificity. Thus, the template for the template-independent 3'-adenylation by Qbeta replicase is the RNA and protein ribonucleoprotein complex.

Mechanism for template-independent terminal adenylation activity of Qbeta replicase.,Takeshita D, Yamashita S, Tomita K Structure. 2012 Oct 10;20(10):1661-9. doi: 10.1016/j.str.2012.07.004. Epub 2012, Aug 9. PMID:22884418<ref>PMID:22884418</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3vnu" style="background-color:#fffaf0;"></div>

==See Also==
*[[Elongation factor 3D structures|Elongation factor 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli O157:H7]]
[[Category: Escherichia virus Qbeta]]
[[Category: Large Structures]]
[[Category: Takeshita D]]
[[Category: Tomita K]]