7xt4: Difference between revisions
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==Structure of Craspase-NTR== | |||
<StructureSection load='7xt4' size='340' side='right'caption='[[7xt4]], [[Resolution|resolution]] 3.08Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7xt4]] 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=7XT4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XT4 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> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7xt4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xt4 OCA], [https://pdbe.org/7xt4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xt4 RCSB], [https://www.ebi.ac.uk/pdbsum/7xt4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xt4 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A0B0EKL4_9BACT A0A0B0EKL4_9BACT] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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 Oct 21. pii: S1097-2765(22)00964-9. doi:, 10.1016/j.molcel.2022.10.007. PMID:36306795<ref>PMID:36306795</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7xt4" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Candidatus Scalindua brodae]] | |||
[[Category: Large Structures]] | |||
[[Category: Laixing Z]] | |||
[[Category: Yue F]] | |||
Revision as of 10:27, 9 November 2022
Structure of Craspase-NTRStructure of Craspase-NTR
Structural highlights
FunctionPublication Abstract from PubMedIn 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 Oct 21. pii: S1097-2765(22)00964-9. doi:, 10.1016/j.molcel.2022.10.007. PMID:36306795[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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