6t0w

<table><tr><td colspan='2'>[[6t0w]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/9infb 9infb]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T0W OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6T0W FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11520 9INFB]), PB1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11520 9INFB]), PB2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11520 9INFB])</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://proteopedia.org/fgij/fg.htm?mol=6t0w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t0w OCA], [http://pdbe.org/6t0w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6t0w RCSB], [http://www.ebi.ac.uk/pdbsum/6t0w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6t0w ProSAT]</span></td></tr>

== Function ==

[[http://www.uniprot.org/uniprot/A0A4Y5WMY1_9INFB A0A4Y5WMY1_9INFB]] Plays an essential role in transcription initiation and cap-stealing mechanism, in which cellular capped pre-mRNAs are used to generate primers for viral transcription. Recognizes and binds a wide range of cap structures of target pre-RNAs which are subsequently cleaved after 10-13 nucleotides by the viral protein PA. Plays a role in the initiation of the viral genome replication and modulates the activity of the ribonucleoprotein (RNP) complex.[HAMAP-Rule:MF_04062]

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== Publication Abstract from PubMed ==

Influenza polymerase uses unique mechanisms to synthesize capped and polyadenylated mRNAs from the genomic viral RNA (vRNA) template, which is packaged inside ribonucleoprotein particles (vRNPs). Here, we visualize by cryoelectron microscopy the conformational dynamics of the polymerase during the complete transcription cycle from pre-initiation to termination, focusing on the template trajectory. After exiting the active site cavity, the template 3' extremity rebinds into a specific site on the polymerase surface. Here, it remains sequestered during all subsequent transcription steps, forcing the template to loop out as it further translocates. At termination, the strained connection between the bound template 5' end and the active site results in polyadenylation by stuttering at uridine 17. Upon product dissociation, further conformational changes release the trapped template, allowing recycling back into the pre-initiation state. Influenza polymerase thus performs transcription while tightly binding to and protecting both template ends, allowing efficient production of multiple mRNAs from a single vRNP.

 

== References ==

[[Category: Cusack, S]]

[[Category: Karuppasamy, M]]

[[Category: Kouba, T]]

[[Category: Wandzik, J M]]

[[Category: Viral transcription]]