7qqk: Difference between revisions

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== Function ==

[[https://www.uniprot.org/uniprot/A0A0M2HE71_9MICO A0A0M2HE71_9MICO]]

== Publication Abstract from PubMed ==

Cyclic nucleotide signalling is a key component of antiviral defence in all domains of life. Viral detection activates a nucleotide cyclase to generate a second messenger, resulting in activation of effector proteins. This is exemplified by the metazoan cGAS-STING innate immunity pathway(1), which originated in bacteria(2). These defence systems require a sensor domain to bind the cyclic nucleotide and are often coupled with an effector domain that, when activated, causes cell death by destroying essential biomolecules(3). One example is the Toll/interleukin-1 receptor (TIR) domain, which degrades the essential cofactor NAD(+) when activated in response to infection in plants and bacteria(2,4,5) or during programmed nerve cell death(6). Here we show that a bacterial antiviral defence system generates a cyclic tri-adenylate that binds to a TIR-SAVED effector, acting as the 'glue' to allow assembly of an extended superhelical solenoid structure. Adjacent TIR subunits interact to organize and complete a composite active site, allowing NAD(+) degradation. Activation requires extended filament formation, both in vitro and in vivo. Our study highlights an example of large-scale molecular assembly controlled by cyclic nucleotides and reveals key details of the mechanism of TIR enzyme activation.

Cyclic nucleotide-induced helical structure activates a TIR immune effector.,Hogrel G, Guild A, Graham S, Rickman H, Gruschow S, Bertrand Q, Spagnolo L, White MF Nature. 2022 Aug;608(7924):808-812. doi: 10.1038/s41586-022-05070-9. Epub 2022, Aug 10. PMID:35948638<ref>PMID:35948638</ref>

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

== References ==

__TOC__

</StructureSection>

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@@ Line 8: / Line 8: @@
 == Function ==
 [[https://www.uniprot.org/uniprot/A0A0M2HE71_9MICO A0A0M2HE71_9MICO]]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Cyclic nucleotide signalling is a key component of antiviral defence in all domains of life. Viral detection activates a nucleotide cyclase to generate a second messenger, resulting in activation of effector proteins. This is exemplified by the metazoan cGAS-STING innate immunity pathway(1), which originated in bacteria(2). These defence systems require a sensor domain to bind the cyclic nucleotide and are often coupled with an effector domain that, when activated, causes cell death by destroying essential biomolecules(3). One example is the Toll/interleukin-1 receptor (TIR) domain, which degrades the essential cofactor NAD(+) when activated in response to infection in plants and bacteria(2,4,5) or during programmed nerve cell death(6). Here we show that a bacterial antiviral defence system generates a cyclic tri-adenylate that binds to a TIR-SAVED effector, acting as the 'glue' to allow assembly of an extended superhelical solenoid structure. Adjacent TIR subunits interact to organize and complete a composite active site, allowing NAD(+) degradation. Activation requires extended filament formation, both in vitro and in vivo. Our study highlights an example of large-scale molecular assembly controlled by cyclic nucleotides and reveals key details of the mechanism of TIR enzyme activation.
+Cyclic nucleotide-induced helical structure activates a TIR immune effector.,Hogrel G, Guild A, Graham S, Rickman H, Gruschow S, Bertrand Q, Spagnolo L, White MF Nature. 2022 Aug;608(7924):808-812. doi: 10.1038/s41586-022-05070-9. Epub 2022, Aug 10. PMID:35948638<ref>PMID:35948638</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 7qqk" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>