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7n35
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of Yersinia aleksiciae Cap15 cyclic dinucleotide receptor, crystal form 2== | |
| + | <StructureSection load='7n35' size='340' side='right'caption='[[7n35]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7n35]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Yersinia_aleksiciae Yersinia aleksiciae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7N35 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7N35 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]] 2.6Å</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=7n35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7n35 OCA], [https://pdbe.org/7n35 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7n35 RCSB], [https://www.ebi.ac.uk/pdbsum/7n35 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7n35 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Cyclic oligonucleotide-based antiphage signaling systems (CBASS) are antiviral defense operons that protect bacteria from phage replication. Here, we discover a widespread class of CBASS transmembrane (TM) effector proteins that respond to antiviral nucleotide signals and limit phage propagation through direct membrane disruption. Crystal structures of the Yersinia TM effector Cap15 reveal a compact 8-stranded beta-barrel scaffold that forms a cyclic dinucleotide receptor domain that oligomerizes upon activation. We demonstrate that activated Cap15 relocalizes throughout the cell and specifically induces rupture of the inner membrane. Screening for active effectors, we identify the function of distinct families of CBASS TM effectors and demonstrate that cell death via disruption of inner-membrane integrity is a common mechanism of defense. Our results reveal the function of the most prominent class of effector protein in CBASS immunity and define disruption of the inner membrane as a widespread strategy of abortive infection in bacterial phage defense. | ||
| - | + | Effector-mediated membrane disruption controls cell death in CBASS antiphage defense.,Duncan-Lowey B, McNamara-Bordewick NK, Tal N, Sorek R, Kranzusch PJ Mol Cell. 2021 Nov 9. pii: S1097-2765(21)00912-6. doi:, 10.1016/j.molcel.2021.10.020. PMID:34784509<ref>PMID:34784509</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 7n35" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Yersinia aleksiciae]] | ||
| + | [[Category: Duncan-Lowey B]] | ||
| + | [[Category: Kranzusch PJ]] | ||
| + | [[Category: McNamara-Bordewick NK]] | ||
Current revision
Structure of Yersinia aleksiciae Cap15 cyclic dinucleotide receptor, crystal form 2
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