5cfo: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5cfo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Nematostella_vectensis Nematostella vectensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CFO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CFO FirstGlance]. <br>
<table><tr><td colspan='2'>[[5cfo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Nematostella_vectensis Nematostella vectensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CFO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CFO 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=5cfo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cfo OCA], [https://pdbe.org/5cfo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cfo RCSB], [https://www.ebi.ac.uk/pdbsum/5cfo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cfo ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.102&#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=5cfo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cfo OCA], [https://pdbe.org/5cfo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cfo RCSB], [https://www.ebi.ac.uk/pdbsum/5cfo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cfo ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/STING_NEMVE STING_NEMVE] Sensor of cytosolic DNA from bacteria and viruses that promotes autophagy (PubMed:30842662). Acts by recognizing and binding cyclic GMP-AMP (cGAMP), a messenger produced by CGAS in response to DNA in the cytosol (PubMed:26300263, PubMed:30842662). Following cGAMP-binding, promotes the formation of autophagosomes, leading to target cytosolic DNA for degradation by the lysosome (PubMed:30842662). Exhibits guanine base-specific ligand recognition. Binds 3'-3'linked cGAMP, 2'-3' linked cGAMP and 3'-3' linked c-di-GMP with much greater affinity as compared to 3'-3' linked c-di-AMP (PubMed:26300263). Lacks the C-terminal tail (CTT) found in mammalian orthologs which is essential for interferon signaling (PubMed:26300263).<ref>PMID:26300263</ref> <ref>PMID:30842662</ref>  
[https://www.uniprot.org/uniprot/STING_NEMVE STING_NEMVE] Sensor of cytosolic DNA from bacteria and viruses that promotes autophagy (PubMed:30842662). Acts by recognizing and binding cyclic GMP-AMP (cGAMP), a messenger produced by CGAS in response to DNA in the cytosol (PubMed:26300263, PubMed:30842662). Following cGAMP-binding, promotes the formation of autophagosomes, leading to target cytosolic DNA for degradation by the lysosome (PubMed:30842662). Exhibits guanine base-specific ligand recognition. Binds 3'-3'linked cGAMP, 2'-3' linked cGAMP and 3'-3' linked c-di-GMP with much greater affinity as compared to 3'-3' linked c-di-AMP (PubMed:26300263). Lacks the C-terminal tail (CTT) found in mammalian orthologs which is essential for interferon signaling (PubMed:26300263).<ref>PMID:26300263</ref> <ref>PMID:30842662</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In humans, the cGAS-STING immunity pathway signals in response to cytosolic DNA via 2',3' cGAMP, a cyclic dinucleotide (CDN) second messenger containing mixed 2'-5' and 3'-5' phosphodiester bonds. Prokaryotes also produce CDNs, but these are exclusively 3' linked, and thus the evolutionary origins of human 2',3' cGAMP signaling are unknown. Here we illuminate the ancient origins of human cGAMP signaling by discovery of a functional cGAS-STING pathway in Nematostella vectensis, an anemone species &gt;500 million years diverged from humans. Anemone cGAS appears to produce a 3',3' CDN that anemone STING recognizes through nucleobase-specific contacts not observed in human STING. Nevertheless, anemone STING binds mixed-linkage 2',3' cGAMP indistinguishably from human STING, trapping a unique structural conformation not induced by 3',3' CDNs. These results reveal that human mixed-linkage cGAMP achieves universal signaling by exploiting a deeply conserved STING conformational intermediate, providing critical insight for therapeutic targeting of the STING pathway.
Ancient Origin of cGAS-STING Reveals Mechanism of Universal 2',3' cGAMP Signaling.,Kranzusch PJ, Wilson SC, Lee AS, Berger JM, Doudna JA, Vance RE Mol Cell. 2015 Aug 19. pii: S1097-2765(15)00580-8. doi:, 10.1016/j.molcel.2015.07.022. PMID:26300263<ref>PMID:26300263</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5cfo" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==

Latest revision as of 12:20, 6 March 2024

Crystal structure of anemone STING (Nematostella vectensis) in apo 'rotated' open conformation

5cfo, resolution 2.10Å

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