8z3p: Difference between revisions
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The | ==The structure of type III CRISPR-associated deaminase in complex cA6 and ATP, fully activated== | ||
<StructureSection load='8z3p' size='340' side='right'caption='[[8z3p]], [[Resolution|resolution]] 3.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8z3p]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Limisphaera_ngatamarikiensis Limisphaera ngatamarikiensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8Z3P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8Z3P FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.4Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <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=8z3p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8z3p OCA], [https://pdbe.org/8z3p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8z3p RCSB], [https://www.ebi.ac.uk/pdbsum/8z3p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8z3p ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A6M1RED6_9BACT A0A6M1RED6_9BACT] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Prokaryotes have evolved diverse defense strategies against viral infection, such as foreign nucleic acid degradation by CRISPR-Cas systems and DNA/RNA synthesis inhibition via nucleotide pool depletion. Here, we report an antiviral mechanism of type III CRISPR-Cas-regulated ATP depletion, where ATP is converted into ITP by CRISPR-Cas-associated adenosine deaminase (CAAD) upon activation by either cA(4) or cA(6), followed by hydrolysis into IMP by Nudix hydrolase, ultimately resulting in cell growth arrest. The cryo-electron microscopy structures of CAAD in its apo and activated forms, together with biochemical evidence, revealed how cA(4)/cA(6) binds to the CARF domain and abrogates CAAD autoinhibition, inducing substantial conformational changes that reshape the structure of CAAD and induce its deaminase activity. Our results reveal the mechanism of a CRISPR-Cas-regulated ATP depletion antiviral strategy. | |||
Antiviral signaling of a type III CRISPR-associated deaminase.,Li Y, Li Z, Yan P, Hua C, Kong J, Wu W, Cui Y, Duan Y, Li S, Li G, Ji S, Chen Y, Zhao Y, Yang P, Hu C, Lu M, Chen M, Xiao Y Science. 2024 Dec 12:eadr0393. doi: 10.1126/science.adr0393. PMID:39666823<ref>PMID:39666823</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8z3p" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Limisphaera ngatamarikiensis]] | |||
[[Category: Chen MR]] | |||
[[Category: Li ZX]] | |||
[[Category: Xiao YB]] | |||
Latest revision as of 12:30, 25 December 2024
The structure of type III CRISPR-associated deaminase in complex cA6 and ATP, fully activatedThe structure of type III CRISPR-associated deaminase in complex cA6 and ATP, fully activated
Structural highlights
FunctionPublication Abstract from PubMedProkaryotes have evolved diverse defense strategies against viral infection, such as foreign nucleic acid degradation by CRISPR-Cas systems and DNA/RNA synthesis inhibition via nucleotide pool depletion. Here, we report an antiviral mechanism of type III CRISPR-Cas-regulated ATP depletion, where ATP is converted into ITP by CRISPR-Cas-associated adenosine deaminase (CAAD) upon activation by either cA(4) or cA(6), followed by hydrolysis into IMP by Nudix hydrolase, ultimately resulting in cell growth arrest. The cryo-electron microscopy structures of CAAD in its apo and activated forms, together with biochemical evidence, revealed how cA(4)/cA(6) binds to the CARF domain and abrogates CAAD autoinhibition, inducing substantial conformational changes that reshape the structure of CAAD and induce its deaminase activity. Our results reveal the mechanism of a CRISPR-Cas-regulated ATP depletion antiviral strategy. Antiviral signaling of a type III CRISPR-associated deaminase.,Li Y, Li Z, Yan P, Hua C, Kong J, Wu W, Cui Y, Duan Y, Li S, Li G, Ji S, Chen Y, Zhao Y, Yang P, Hu C, Lu M, Chen M, Xiao Y Science. 2024 Dec 12:eadr0393. doi: 10.1126/science.adr0393. PMID:39666823[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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