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'''Unreleased structure'''


The entry 9pft is ON HOLD  until Paper Publication
==Cryo-EM structure of the respiratory syncytial virus polymerase (L:P) in pre-translocation elongation state==
<StructureSection load='9pft' size='340' side='right'caption='[[9pft]], [[Resolution|resolution]] 3.07&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9pft]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Respiratory_syncytial_virus_A2 Respiratory syncytial virus A2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9PFT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9PFT FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.07&#8491;</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=9pft FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9pft OCA], [https://pdbe.org/9pft PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9pft RCSB], [https://www.ebi.ac.uk/pdbsum/9pft PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9pft ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The respiratory syncytial virus (RSV) polymerase (L:P complex) is responsible for viral RNA transcription and replication, where nucleotide addition cycles (NACs) are executed repeatedly during elongation in both processes. Using cryo-EM, we capture snapshots of RSV polymerase in action during early-stage elongation and in four distinct NAC states: NTP-bound, pre-reaction, pre-translocation, and post-translocation. Strikingly, we observe all five domains of RSV L in NTP-bound and post-translocation states. In contrast, only two domains are visible in pre-reaction and pre-translocation states, similar to previously reported apo or promoter-bound structures. Importantly, these snapshots reveal the synergistic and dynamic interaction networks among key residues and motifs of RSV polymerase, RNA template, product, incoming nucleotide, and metal ions across NAC states. Our findings provide the first comprehensive insights into orchestrated macro-domain rearrangements and micro-motif changes of RSV polymerase during NAC catalysis, facilitating antiviral therapeutics targeting RSV and related nonsegmented negative-sense RNA viruses, including rabies, Nipah, and Ebola.


Authors:  
Orchestrated and dynamic nucleotide addition cycle during respiratory syncytial virus early-stage elongation.,Cao D, Chen Z, Gao Y, Roesler C, Gooneratne I, Mera C, Zhuang L, Slack J, Nudell-Cook E, Vy J, Berry J, Royal M, Shaik M, Youngs R, Liang B Nat Commun. 2026 Apr 29. doi: 10.1038/s41467-026-72519-0. PMID:42049741<ref>PMID:42049741</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 9pft" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Respiratory syncytial virus A2]]
[[Category: Cao D]]
[[Category: Chen Z]]
[[Category: Gao Y]]
[[Category: Gooneratne I]]
[[Category: Liang B]]
[[Category: Roesler C]]
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