1wac: Difference between revisions

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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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[[Image:1wac.gif|left|200px]]<br /><applet load="1wac" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1wac.gif|left|200px]]<br /><applet load="1wac" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1wac, resolution 3.0&Aring;" />
caption="1wac, resolution 3.0&Aring;" />
'''BACK-PRIMING MODE OF PHI6 RNA-DEPENDENT RNA POLYMERASE'''<br />
'''BACK-PRIMING MODE OF PHI6 RNA-DEPENDENT RNA POLYMERASE'''<br />


==Overview==
==Overview==
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.
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.


==About this Structure==
==About this Structure==
1WAC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_phi-6 Bacteriophage phi-6]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WAC OCA].  
1WAC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_phi-6 Bacteriophage phi-6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WAC OCA].  


==Reference==
==Reference==
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[[Category: Bacteriophage phi-6]]
[[Category: Bacteriophage phi-6]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Bamford, D.H.]]
[[Category: Bamford, D H.]]
[[Category: Grimes, J.M.]]
[[Category: Grimes, J M.]]
[[Category: Laurila, M.R.L.]]
[[Category: Laurila, M R.L.]]
[[Category: Salgado, P.S.]]
[[Category: Salgado, P S.]]
[[Category: Stuart, D.I.]]
[[Category: Stuart, D I.]]
[[Category: phi6 rna-dependent rna polymerase]]
[[Category: phi6 rna-dependent rna polymerase]]
[[Category: transcription]]
[[Category: transcription]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:16:39 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:42:08 2008''

Revision as of 16:42, 21 February 2008

File:1wac.gif


1wac, resolution 3.0Å

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BACK-PRIMING MODE OF PHI6 RNA-DEPENDENT RNA POLYMERASE

OverviewOverview

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.

About this StructureAbout this Structure

1WAC is a Single protein structure of sequence from Bacteriophage phi-6. Full crystallographic information is available from OCA.

ReferenceReference

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

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