View source for 6ae4


==Crystals structure of Classical swine fever virus NS5B (residues 1-694, Y471A mutant)==
<StructureSection load='6ae4' size='340' side='right'caption='[[6ae4]], [[Resolution|resolution]] 2.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6ae4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Classical_swine_fever_virus Classical swine fever virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AE4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6AE4 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.95&#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=6ae4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ae4 OCA], [https://pdbe.org/6ae4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ae4 RCSB], [https://www.ebi.ac.uk/pdbsum/6ae4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ae4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q5U8X5_9FLAV Q5U8X5_9FLAV] 
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== Publication Abstract from PubMed ==
Typically not assisted by proofreading, the RNA-dependent RNA polymerases (RdRPs) encoded by the RNA viruses may need to independently control its fidelity to fulfill virus viability and fitness. However, the precise mechanism by which the RdRP maintains its optimal fidelity level remains largely elusive. By solving 2.1-2.5 A resolution crystal structures of the classical swine fever virus (CSFV) NS5B, an RdRP with a unique naturally fused N-terminal domain (NTD), we identified high-resolution intra-molecular interactions between the NTD and the RdRP palm domain. In order to dissect possible regulatory functions of NTD, we designed mutations at residues Y471 and E472 to perturb key interactions at the NTD-RdRP interface. When crystallized, some of these NS5B interface mutants maintained the interface, while the others adopted an 'open' conformation that no longer retained the intra-molecular interactions. Data from multiple in vitro RdRP assays indicated that the perturbation of the NTD-RdRP interactions clearly reduced the fidelity level of the RNA synthesis, while the processivity of the NS5B elongation complex was not affected. Collectively, our work demonstrates an explicit and unique mode of polymerase fidelity modulation and provides a vivid example of co-evolution in multi-domain enzymes.

A unique intra-molecular fidelity-modulating mechanism identified in a viral RNA-dependent RNA polymerase.,Liu W, Shi X, Gong P Nucleic Acids Res. 2018 Sep 20. pii: 5103954. doi: 10.1093/nar/gky848. PMID:30239956<ref>PMID:30239956</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6ae4" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Classical swine fever virus]]
[[Category: Large Structures]]
[[Category: Gong P]]
[[Category: Liu W]]