6xb5
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of Trichoplusia ni poxin in post-reactive state with Gp[2'-5']Ap[3']== | |
| + | <StructureSection load='6xb5' size='340' side='right'caption='[[6xb5]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6xb5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichoplusia_ni Trichoplusia ni]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XB5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XB5 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]] 2.9Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9BG:2,5-GpAp'>9BG</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=6xb5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xb5 OCA], [https://pdbe.org/6xb5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xb5 RCSB], [https://www.ebi.ac.uk/pdbsum/6xb5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xb5 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A7E5VPD6_TRINI A0A7E5VPD6_TRINI] Nuclease that cleaves 2',3'-cGAMP.[HAMAP-Rule:MF_04143] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | DNA viruses in the family Poxviridae encode poxin enzymes that degrade the immune second messenger 2'3'-cGAMP to inhibit cGAS-STING immunity in mammalian cells. The closest homologs of poxin exist in the genomes of insect viruses suggesting a key mechanism of cGAS-STING evasion may have evolved outside of mammalian biology. Here we use a biochemical and structural approach to discover a broad family of 369 poxins encoded in diverse viral and animal genomes and define a prominent role for 2'3'-cGAMP cleavage in metazoan host-pathogen conflict. Structures of insect poxins reveal unexpected homology to flavivirus proteases and enable identification of functional self-cleaving poxins in RNA virus polyproteins. Our data suggest widespread 2'3'-cGAMP signaling in insect antiviral immunity and explain how a family of cGAS-STING evasion enzymes evolved from viral proteases through gain of secondary nuclease activity. Poxin acquisition by poxviruses demonstrates the importance of environmental connections in shaping evolution of mammalian pathogens. | ||
| - | + | Structures of diverse poxin cGAMP nucleases reveal a widespread role for cGAS-STING evasion in host-pathogen conflict.,Eaglesham JB, McCarty KL, Kranzusch PJ Elife. 2020 Nov 16;9. pii: 59753. doi: 10.7554/eLife.59753. PMID:33191912<ref>PMID:33191912</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6xb5" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Trichoplusia ni]] | ||
| + | [[Category: Eaglesham JB]] | ||
| + | [[Category: Kranzusch PJ]] | ||
| + | [[Category: McCarty KL]] | ||
Current revision
Structure of Trichoplusia ni poxin in post-reactive state with Gp[2'-5']Ap[3']
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