7xss
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7xss]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Candidatus_Scalindua_brodae Candidatus Scalindua brodae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7XSS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XSS FirstGlance]. <br> | <table><tr><td colspan='2'>[[7xss]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Candidatus_Scalindua_brodae Candidatus Scalindua brodae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7XSS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XSS FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.2Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=7xss FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xss OCA], [https://pdbe.org/7xss PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xss RCSB], [https://www.ebi.ac.uk/pdbsum/7xss PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xss ProSAT]</span></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=7xss FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xss OCA], [https://pdbe.org/7xss PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xss RCSB], [https://www.ebi.ac.uk/pdbsum/7xss PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xss ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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In the type III-E CRISPR-Cas system, a Cas effector (gRAMP) is associated with a TPR-CHAT to form Craspase (CRISPR-guided caspase). However, both the structural features of gRAMP and the immunity mechanism remain unknown for this system. Here, we report structures of gRAMP-crRNA and gRAMP:cRNA:target RNA as well as structures of Craspase and Craspase complexed with cognate target RNA (CTR) or non-cognate target RNA (NTR). Importantly, the 3' anti-tag region of NTR and CTR binds at two distinct channels in Craspase, and CTR with a non-complementary 3' anti-tag induces a marked conformational change of the TPR-CHAT, which allosterically activates its protease activity to cleave an ancillary protein Csx30. This cleavage then triggers an abortive infection as the antiviral strategy of the type III-E system. Together, our study provides crucial insights into both the catalytic mechanism of the gRAMP and the immunity mechanism of the type III-E system. | In the type III-E CRISPR-Cas system, a Cas effector (gRAMP) is associated with a TPR-CHAT to form Craspase (CRISPR-guided caspase). However, both the structural features of gRAMP and the immunity mechanism remain unknown for this system. Here, we report structures of gRAMP-crRNA and gRAMP:cRNA:target RNA as well as structures of Craspase and Craspase complexed with cognate target RNA (CTR) or non-cognate target RNA (NTR). Importantly, the 3' anti-tag region of NTR and CTR binds at two distinct channels in Craspase, and CTR with a non-complementary 3' anti-tag induces a marked conformational change of the TPR-CHAT, which allosterically activates its protease activity to cleave an ancillary protein Csx30. This cleavage then triggers an abortive infection as the antiviral strategy of the type III-E system. Together, our study provides crucial insights into both the catalytic mechanism of the gRAMP and the immunity mechanism of the type III-E system. | ||
| - | Target RNA activates the protease activity of Craspase to confer antiviral defense.,Liu X, Zhang L, Wang H, Xiu Y, Huang L, Gao Z, Li N, Li F, Xiong W, Gao T, Zhang Y, Yang M, Feng Y Mol Cell. 2022 | + | Target RNA activates the protease activity of Craspase to confer antiviral defense.,Liu X, Zhang L, Wang H, Xiu Y, Huang L, Gao Z, Li N, Li F, Xiong W, Gao T, Zhang Y, Yang M, Feng Y Mol Cell. 2022 Dec 1;82(23):4503-4518.e8. doi: 10.1016/j.molcel.2022.10.007. Epub , 2022 Oct 27. PMID:36306795<ref>PMID:36306795</ref> |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
Current revision
Structure of Craspase-CTR
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