6wt8
From Proteopedia
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| - | ==Structure of a STING-associated CdnE c-di-GMP synthase from | + | ==Structure of a STING-associated CdnE c-di-GMP synthase from Flacobacteriaceae sp.== |
<StructureSection load='6wt8' size='340' side='right'caption='[[6wt8]], [[Resolution|resolution]] 1.52Å' scene=''> | <StructureSection load='6wt8' size='340' side='right'caption='[[6wt8]], [[Resolution|resolution]] 1.52Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'> | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6WT8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6WT8 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.52Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=6wt8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wt8 OCA], [https://pdbe.org/6wt8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6wt8 RCSB], [https://www.ebi.ac.uk/pdbsum/6wt8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6wt8 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Stimulator of interferon genes (STING) is a receptor in human cells that senses foreign cyclic dinucleotides released during bacterial infection and endogenous cyclic GMP-AMP signalling during viral infection and antitumour immunity(1-5). STING shares no structural homology with other known signalling proteins(6-9), limiting functional analysis and preventing explanation of the origin of cyclic dinucleotide signalling in mammalian innate immunity. Here we discover functional STING homologues encoded within prokaryotic defence islands and reveal a conserved mechanism of signal activation. Crystal structures of bacterial STING define a minimal homodimeric scaffold that selectively responds to c-di-GMP synthesized by a neighbouring cGAS/DncV-like nucleotidyltransferase (CD-NTase) enzyme. Bacterial STING domains couple cyclic dinucleotide recognition with protein filament formation to drive TIR effector domain oligomerization and rapid NAD(+) cleavage. We reconstruct the evolutionary events following acquisition of STING into metazoan innate immunity and determine the structure of a full-length TIR-STING fusion from the Pacific oyster Crassostrea gigas. Comparative structural analysis demonstrates how metazoan-specific additions to the core STING scaffold enabled a switch from direct effector function to regulation of antiviral transcription. Together, our results explain the mechanism of STING-dependent signalling and reveal conservation of a functional cGAS-STING pathway in prokaryotic bacteriophage defence. | ||
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| - | STING cyclic dinucleotide sensing originated in bacteria.,Morehouse BR, Govande AA, Millman A, Keszei AFA, Lowey B, Ofir G, Shao S, Sorek R, Kranzusch PJ Nature. 2020 Sep 2. pii: 10.1038/s41586-020-2719-5. doi:, 10.1038/s41586-020-2719-5. PMID:32877915<ref>PMID:32877915</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 6wt8" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Flavobacteriaceae bacterium]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Govande | + | [[Category: Govande AA]] |
| - | [[Category: Keszei | + | [[Category: Keszei AFA]] |
| - | [[Category: Kranzusch | + | [[Category: Kranzusch PJ]] |
| - | [[Category: Lowey | + | [[Category: Lowey B]] |
| - | [[Category: Millman | + | [[Category: Millman A]] |
| - | [[Category: Morehouse | + | [[Category: Morehouse BR]] |
| - | [[Category: Ofir | + | [[Category: Ofir G]] |
| - | [[Category: Shao | + | [[Category: Shao S]] |
| - | [[Category: Sorek | + | [[Category: Sorek R]] |
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Current revision
Structure of a STING-associated CdnE c-di-GMP synthase from Flacobacteriaceae sp.
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Categories: Large Structures | Govande AA | Keszei AFA | Kranzusch PJ | Lowey B | Millman A | Morehouse BR | Ofir G | Shao S | Sorek R
