5vim: Difference between revisions

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New page: '''Unreleased structure''' The entry 5vim is ON HOLD Authors: Bukrejewska, M., Derewenda, Z.S., Derewenda, U. Description: Crystal structure of the Zika virus NS5 methyltransferase. [[...
 
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'''Unreleased structure'''


The entry 5vim is ON HOLD
==Crystal structure of the Zika virus NS5 methyltransferase.==
<StructureSection load='5vim' size='340' side='right'caption='[[5vim]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5vim]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Zika_virus Zika virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VIM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VIM 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]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=5vim FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vim OCA], [https://pdbe.org/5vim PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vim RCSB], [https://www.ebi.ac.uk/pdbsum/5vim PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vim ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/POLG_ZIKV POLG_ZIKV] Protein C: Encapsulates the genomic RNA.[UniProtKB:P17763]  prM: Acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is matured in the last step of virion assembly, presumably to avoid catastrophic activation of the viral fusion peptide induced by the acidic pH of the trans-Golgi network. After cleavage by host furin, the pr peptide is released in the extracellular medium and small envelope protein M and envelope protein E homodimers are dissociated.[UniProtKB:P17763]  Envelope protein E: Binding to host cell surface receptor is followed by virus internalization through clathrin-mediated endocytosis. Envelope protein E is subsequently involved in membrane fusion between virion and host late endosomes. Synthesized as a homodimer with prM which acts as a chaperone for envelope protein E. After cleavage of prM, envelope protein E dissociate from small envelope protein M and homodimerizes.[UniProtKB:P17763]  Non-structural protein 1: Involved in virus replication and regulation of the innate immune response.[UniProtKB:P17763]  Non-structural protein 2A: May be involved viral RNA replication and capsid assembly.[UniProtKB:P09732]  Non-structural protein 4A: Induces host endoplasmic reticulum membrane rearrangements leading to the formation of virus-induced membranous vesicles hosting the dsRNA and polymerase, functioning as a replication complex. NS4A might also regulate the ATPase activity of the helicase region of Serine protease NS3 chain.[UniProtKB:P17763]  Peptide 2k: Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter.[UniProtKB:P17763]  Non-structural protein 4B: Inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway.[UniProtKB:P17763]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Two nonstructural proteins encoded by Zika virus strain MR766 RNA, a methyltransferase and a helicase, were crystallized and their structures were solved and refined at 2.10 and 2.01 A resolution, respectively. The NS5 methyltransferase contains a bound S-adenosyl-L-methionine (SAM) co-substrate. The NS3 helicase is in the apo form. Comparison with published crystal structures of the helicase in the apo, nucleotide-bound and single-stranded RNA (ssRNA)-bound states suggests that binding of ssRNA to the helicase may occur through conformational selection rather than induced fit.


Authors: Bukrejewska, M., Derewenda, Z.S., Derewenda, U.
Crystal structures of the methyltransferase and helicase from the ZIKA 1947 MR766 Uganda strain.,Bukrejewska M, Derewenda U, Radwanska M, Engel DA, Derewenda ZS Acta Crystallogr D Struct Biol. 2017 Sep 1;73(Pt 9):767-774. doi:, 10.1107/S2059798317010737. Epub 2017 Aug 15. PMID:28876240<ref>PMID:28876240</ref>


Description: Crystal structure of the Zika virus NS5 methyltransferase.
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Derewenda, U]]
<div class="pdbe-citations 5vim" style="background-color:#fffaf0;"></div>
[[Category: Bukrejewska, M]]
== References ==
[[Category: Derewenda, Z.S]]
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Zika virus]]
[[Category: Bukrejewska M]]
[[Category: Derewenda U]]
[[Category: Derewenda ZS]]

Latest revision as of 13:49, 4 October 2023

Crystal structure of the Zika virus NS5 methyltransferase.

5vim, resolution 2.10Å

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