3avy: Difference between revisions
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< | ==Structure of viral RNA polymerase complex 6== | ||
<StructureSection load='3avy' size='340' side='right'caption='[[3avy]], [[Resolution|resolution]] 2.62Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3avy]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7], [https://en.wikipedia.org/wiki/Escherichia_virus_Qbeta Escherichia virus Qbeta] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AVY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AVY 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]] 2.616Å</td></tr> | |||
-- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CH1:3-DEOXY-CYTIDINE-5-TRIPHOSPHATE'>CH1</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=3avy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3avy OCA], [https://pdbe.org/3avy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3avy RCSB], [https://www.ebi.ac.uk/pdbsum/3avy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3avy 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 == | |||
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> | |||
<div class="pdbe-citations 3avy" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
[[ | *[[Elongation factor 3D structures|Elongation factor 3D structures]] | ||
[[Category: Escherichia coli | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli O157:H7]] | ||
[[Category: | [[Category: Escherichia virus Qbeta]] | ||
[[Category: Large Structures]] | |||
[[Category: Synthetic construct]] | |||
[[Category: Takeshita D]] | |||
[[Category: Tomita K]] | |||
Latest revision as of 15:58, 4 October 2023
Structure of viral RNA polymerase complex 6
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