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==X-ray crystal structure of Viperin-like enzyme from Nematostella vectensis==
==X-ray crystal structure of Viperin-like enzyme from Nematostella vectensis==
<StructureSection load='7n7h' size='340' side='right'caption='[[7n7h]]' scene=''>
<StructureSection load='7n7h' size='340' side='right'caption='[[7n7h]], [[Resolution|resolution]] 1.42&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7N7H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7N7H FirstGlance]. <br>
<table><tr><td colspan='2'>[[7n7h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Nemve Nemve]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7N7H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7N7H FirstGlance]. <br>
</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=7n7h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7n7h OCA], [https://pdbe.org/7n7h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7n7h RCSB], [https://www.ebi.ac.uk/pdbsum/7n7h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7n7h ProSAT]</span></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CTP:CYTIDINE-5-TRIPHOSPHATE'>CTP</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">v1g87644 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=45351 NEMVE])</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=7n7h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7n7h OCA], [https://pdbe.org/7n7h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7n7h RCSB], [https://www.ebi.ac.uk/pdbsum/7n7h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7n7h ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Viperin is a member of the radical S-adenosylmethionine superfamily and has been shown to restrict the replication of a wide range of RNA and DNA viruses. We recently demonstrated that human viperin (HsVip) catalyzes the conversion of CTP to 3'-deoxy-3',4'-didehydro-CTP (ddhCTP or ddh-synthase), which acts as a chain terminator for virally encoded RNA-dependent RNA polymerases from several flaviviruses. Viperin homologues also exist in non-chordate eukaryotes (e.g., Cnidaria and Mollusca), numerous fungi, and members of the archaeal and eubacterial domains. Recently, it was reported that non-chordate and non-eukaryotic viperin-like homologues are also ddh-synthases and generate a diverse range of ddhNTPs, including the newly discovered ddhUTP and ddhGTP. Herein, we expand on the catalytic mechanism of mammalian, fungal, bacterial, and archaeal viperin-like enzymes with a combination of X-ray crystallography and enzymology. We demonstrate that, like mammalian viperins, these recently discovered viperin-like enzymes operate through the same mechanism and can be classified as ddh-synthases. Furthermore, we define the unique chemical and physical determinants supporting ddh-synthase activity and nucleotide selectivity, including the crystallographic characterization of a fungal viperin-like enzyme that utilizes UTP as a substrate and a cnidaria viperin-like enzyme that utilizes CTP as a substrate. Together, these results support the evolutionary conservation of the ddh-synthase activity and its broad phylogenetic role in innate antiviral immunity.
Structural Insight into the Substrate Scope of Viperin and Viperin-like Enzymes from Three Domains of Life.,Lachowicz JC, Gizzi AS, Almo SC, Grove TL Biochemistry. 2021 Jul 6;60(26):2116-2129. doi: 10.1021/acs.biochem.0c00958. Epub, 2021 Jun 22. PMID:34156827<ref>PMID:34156827</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7n7h" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Almo SC]]
[[Category: Nemve]]
[[Category: Bonanno JB]]
[[Category: Almo, S C]]
[[Category: Gizzi AG]]
[[Category: Bonanno, J B]]
[[Category: Grove TL]]
[[Category: Gizzi, A G]]
[[Category: Lachowicz JC]]
[[Category: Grove, T L]]
[[Category: Lachowicz, J C]]
[[Category: Antiviral]]
[[Category: Antiviral protein]]
[[Category: Ddh-synthase]]
[[Category: Metalloprotein]]
[[Category: Radical sam protein]]
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