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New page: left|200px<br /><applet load="1wac" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wac, resolution 3.0Å" /> '''BACK-PRIMING MODE OF ... |
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== | ==Back-priming mode of Phi6 RNA-dependent RNA polymerase== | ||
The RNA-dependent RNA polymerase of the double-stranded RNA bacteriophage | <StructureSection load='1wac' size='340' side='right'caption='[[1wac]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1wac]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_virus_phi6 Pseudomonas virus phi6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WAC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WAC 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]] 3Å</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=1wac FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wac OCA], [https://pdbe.org/1wac PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wac RCSB], [https://www.ebi.ac.uk/pdbsum/1wac PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wac ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/RDRP_BPPH6 RDRP_BPPH6] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The RNA-dependent RNA polymerase of the double-stranded RNA bacteriophage phi6 is capable of primer-independent initiation, as are many RNA polymerases. The structure of this polymerase revealed an initiation platform, composed of a loop in the C-terminal domain (QYKW, aa 629-632), that was essential for de novo initiation. A similar element has been identified in hepatitis C virus RNA-dependent RNA polymerase. Biochemical studies have addressed the role of this platform, revealing that a mutant version can utilize a back-priming initiation mechanism, where the 3' terminus of the template adopts a hairpin-like conformation. Here, the mechanism of back-primed initiation is studied further by biochemical and structural methods. | |||
Back-priming mode of phi6 RNA-dependent RNA polymerase.,Laurila MR, Salgado PS, Stuart DI, Grimes JM, Bamford DH J Gen Virol. 2005 Feb;86(Pt 2):521-6. PMID:15659773<ref>PMID:15659773</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1wac" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[RNA polymerase 3D structures|RNA polymerase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Pseudomonas virus phi6]] | |||
[[Category: Bamford DH]] | |||
[[Category: Grimes JM]] | |||
[[Category: Laurila MRL]] | |||
[[Category: Salgado PS]] | |||
[[Category: Stuart DI]] | |||
Latest revision as of 14:25, 2 August 2023
Back-priming mode of Phi6 RNA-dependent RNA polymeraseBack-priming mode of Phi6 RNA-dependent RNA polymerase
Structural highlights
FunctionPublication Abstract from PubMedThe RNA-dependent RNA polymerase of the double-stranded RNA bacteriophage phi6 is capable of primer-independent initiation, as are many RNA polymerases. The structure of this polymerase revealed an initiation platform, composed of a loop in the C-terminal domain (QYKW, aa 629-632), that was essential for de novo initiation. A similar element has been identified in hepatitis C virus RNA-dependent RNA polymerase. Biochemical studies have addressed the role of this platform, revealing that a mutant version can utilize a back-priming initiation mechanism, where the 3' terminus of the template adopts a hairpin-like conformation. Here, the mechanism of back-primed initiation is studied further by biochemical and structural methods. Back-priming mode of phi6 RNA-dependent RNA polymerase.,Laurila MR, Salgado PS, Stuart DI, Grimes JM, Bamford DH J Gen Virol. 2005 Feb;86(Pt 2):521-6. PMID:15659773[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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