5fmz: Difference between revisions

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'''Unreleased structure'''
==Crystal structure of Influenza B polymerase with bound 5' vRNA==
<StructureSection load='5fmz' size='340' side='right' caption='[[5fmz]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5fmz]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FMZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FMZ FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5fml|5fml]], [[5fmm|5fmm]], [[5fmq|5fmq]]</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>
<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=5fmz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fmz OCA], [http://pdbe.org/5fmz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fmz RCSB], [http://www.ebi.ac.uk/pdbsum/5fmz PDBsum]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Influenza virus polymerase transcribes or replicates the segmented RNA genome (vRNA) into respectively viral mRNA or full-length copies and initiates RNA synthesis by binding the conserved 3' and 5' vRNA ends (the promoter). In recent structures of promoter-bound polymerase, the cap-binding and endonuclease domains are configured for cap snatching, which generates capped transcription primers. Here, we present a FluB polymerase structure with a bound complementary cRNA 5' end that exhibits a major rearrangement of the subdomains within the C-terminal two-thirds of PB2 (PB2-C). Notably, the PB2 nuclear localization signal (NLS)-containing domain translocates approximately 90 A to bind to the endonuclease domain. FluA PB2-C alone and RNA-free FluC polymerase are similarly arranged. Biophysical and cap-dependent endonuclease assays show that in solution the polymerase explores different conformational distributions depending on which RNA is bound. The inherent flexibility of the polymerase allows it to adopt alternative conformations that are likely important during polymerase maturation into active progeny RNPs.


The entry 5fmz is ON HOLD  until Paper Publication
Influenza Polymerase Can Adopt an Alternative Configuration Involving a Radical Repacking of PB2 Domains.,Thierry E, Guilligay D, Kosinski J, Bock T, Gaudon S, Round A, Pflug A, Hengrung N, El Omari K, Baudin F, Hart DJ, Beck M, Cusack S Mol Cell. 2016 Jan 7;61(1):125-37. doi: 10.1016/j.molcel.2015.11.016. Epub 2015, Dec 17. PMID:26711008<ref>PMID:26711008</ref>


Authors: Guilligay, D., Cusack, S.
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
Description: Crystal structure of Influenza B polymerase with bound 5' vRNA
<div class="pdbe-citations 5fmz" style="background-color:#fffaf0;"></div>
[[Category: Unreleased Structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: RNA-directed RNA polymerase]]
[[Category: Cusack, S]]
[[Category: Cusack, S]]
[[Category: Guilligay, D]]
[[Category: Guilligay, D]]
[[Category: Heterotrimer]]
[[Category: Influenza b virus rna-dependent rna polymerase]]
[[Category: Transcription]]
[[Category: Viral rna]]
[[Category: Vrna 5' end]]

Revision as of 23:10, 13 January 2016

Crystal structure of Influenza B polymerase with bound 5' vRNACrystal structure of Influenza B polymerase with bound 5' vRNA

Structural highlights

5fmz is a 8 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Activity:RNA-directed RNA polymerase, with EC number 2.7.7.48
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum

Publication Abstract from PubMed

Influenza virus polymerase transcribes or replicates the segmented RNA genome (vRNA) into respectively viral mRNA or full-length copies and initiates RNA synthesis by binding the conserved 3' and 5' vRNA ends (the promoter). In recent structures of promoter-bound polymerase, the cap-binding and endonuclease domains are configured for cap snatching, which generates capped transcription primers. Here, we present a FluB polymerase structure with a bound complementary cRNA 5' end that exhibits a major rearrangement of the subdomains within the C-terminal two-thirds of PB2 (PB2-C). Notably, the PB2 nuclear localization signal (NLS)-containing domain translocates approximately 90 A to bind to the endonuclease domain. FluA PB2-C alone and RNA-free FluC polymerase are similarly arranged. Biophysical and cap-dependent endonuclease assays show that in solution the polymerase explores different conformational distributions depending on which RNA is bound. The inherent flexibility of the polymerase allows it to adopt alternative conformations that are likely important during polymerase maturation into active progeny RNPs.

Influenza Polymerase Can Adopt an Alternative Configuration Involving a Radical Repacking of PB2 Domains.,Thierry E, Guilligay D, Kosinski J, Bock T, Gaudon S, Round A, Pflug A, Hengrung N, El Omari K, Baudin F, Hart DJ, Beck M, Cusack S Mol Cell. 2016 Jan 7;61(1):125-37. doi: 10.1016/j.molcel.2015.11.016. Epub 2015, Dec 17. PMID:26711008[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Thierry E, Guilligay D, Kosinski J, Bock T, Gaudon S, Round A, Pflug A, Hengrung N, El Omari K, Baudin F, Hart DJ, Beck M, Cusack S. Influenza Polymerase Can Adopt an Alternative Configuration Involving a Radical Repacking of PB2 Domains. Mol Cell. 2016 Jan 7;61(1):125-37. doi: 10.1016/j.molcel.2015.11.016. Epub 2015, Dec 17. PMID:26711008 doi:http://dx.doi.org/10.1016/j.molcel.2015.11.016

5fmz, resolution 3.40Å

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