View source for 8qdj


==Ntaya virus methyltransferase in complex wih Sinefungin==
<StructureSection load='8qdj' size='340' side='right'caption='[[8qdj]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8qdj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ntaya_virus Ntaya virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8QDJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8QDJ 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]] 1.8&#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=8qdj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8qdj OCA], [https://pdbe.org/8qdj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8qdj RCSB], [https://www.ebi.ac.uk/pdbsum/8qdj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8qdj ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/K0BRZ6_9FLAV K0BRZ6_9FLAV] Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter.[ARBA:ARBA00003504]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Flaviviruses are single-stranded positive-sense RNA (+RNA) viruses that are responsible for several (re)emerging diseases such as yellow, dengue, or West Nile fevers. The Zika epidemic highlighted their dangerousness when a relatively benign virus known since the 1950s turned into a deadly pathogen. The central protein for their replication is NS5 (non-structural protein 5), which is composed of the N-terminal methyltransferase (MTase) domain and the C-terminal RNA-dependent RNA-polymerase (RdRp) domain. It is responsible for both RNA replication and installation of the 5' RNA cap. We structurally and biochemically analyzed the Ntaya virus MTase and RdRp domains and we compared their properties to other flaviviral NS5s. The enzymatic centers are well conserved across Flaviviridae, suggesting that the development of drugs targeting all flaviviruses is feasible. However, the enzymatic activities of the isolated proteins were significantly different for the MTase domains.

Structural and functional insights in flavivirus NS5 proteins gained by the structure of Ntaya virus polymerase and methyltransferase.,Krejcova K, Krafcikova P, Klima M, Chalupska D, Chalupsky K, Zilecka E, Boura E Structure. 2024 May 11:S0969-2126(24)00173-4. doi: 10.1016/j.str.2024.04.020. PMID:38781970<ref>PMID:38781970</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8qdj" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Ntaya virus]]
[[Category: Boura E]]
[[Category: Klima M]]
[[Category: Krejcova K]]