6f5o

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'''Unreleased structure'''
 
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The entry 6f5o is ON HOLD until Paper Publication
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==A mechanism for the activation of the influenza virus transcriptase==
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<StructureSection load='6f5o' size='340' side='right' caption='[[6f5o]], [[Resolution|resolution]] 9.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6f5o]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F5O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6F5O FirstGlance]. <br>
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</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RNA-directed_RNA_polymerase RNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.48 2.7.7.48] </span></td></tr>
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<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=6f5o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f5o OCA], [http://pdbe.org/6f5o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6f5o RCSB], [http://www.ebi.ac.uk/pdbsum/6f5o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6f5o ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Influenza virus RNA polymerase (FluPol), a heterotrimer composed of PB1, PB2, and PA subunits (P3 in influenza C), performs both transcription and replication of the viral RNA genome. For transcription, FluPol interacts with the C-terminal domain (CTD) of RNA polymerase II (Pol II), which enables FluPol to snatch capped RNA primers from nascent host RNAs. Here, we describe the co-crystal structure of influenza C virus polymerase (FluPolC) bound to a Ser5-phosphorylated CTD (pS5-CTD) peptide. The position of the CTD-binding site at the interface of PB1, P3, and the flexible PB2 C-terminal domains suggests that CTD binding stabilizes the transcription-competent conformation of FluPol. In agreement, both cap snatching and capped primer-dependent transcription initiation by FluPolC are enhanced in the presence of pS5-CTD. Mutations of amino acids in the CTD-binding site reduce viral mRNA synthesis. We propose a model for the activation of the influenza virus transcriptase through its association with pS5-CTD of Pol II.
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Authors: Serna Martin, I., Grimes, J.M.
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A Mechanism for the Activation of the Influenza Virus Transcriptase.,Serna Martin I, Hengrung N, Renner M, Sharps J, Martinez-Alonso M, Masiulis S, Grimes JM, Fodor E Mol Cell. 2018 Jun 21;70(6):1101-1110.e4. doi: 10.1016/j.molcel.2018.05.011. Epub, 2018 Jun 14. PMID:29910112<ref>PMID:29910112</ref>
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Description: A mechanism for the activation of the influenza virus transcriptase
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Grimes, J.M]]
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<div class="pdbe-citations 6f5o" style="background-color:#fffaf0;"></div>
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[[Category: Serna Martin, I]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: RNA-directed RNA polymerase]]
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[[Category: Grimes, J M]]
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[[Category: Martin, I Serna]]
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[[Category: Influenza virus rna dependent rna polymerase]]
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[[Category: Viral protein]]

Revision as of 05:39, 27 June 2018

A mechanism for the activation of the influenza virus transcriptase

6f5o, resolution 9.80Å

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