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| <StructureSection load='6sic' size='340' side='right'caption='[[6sic]], [[Resolution|resolution]] 3.52Å' scene=''> | | <StructureSection load='6sic' size='340' side='right'caption='[[6sic]], [[Resolution|resolution]] 3.52Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[6sic]] is a 35 chain structure with sequence from [http://en.wikipedia.org/wiki/ ], [http://en.wikipedia.org/wiki/Sulir Sulir] and [http://en.wikipedia.org/wiki/Sulfolobus_islandicus_rey15a Sulfolobus islandicus rey15a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SIC OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6SIC FirstGlance]. <br> | | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SIC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SIC 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]] 3.52Å</td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SiRe_0602 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=930945 SULIR]), SiRe_0599 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=930945 SULIR])</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'>[http://proteopedia.org/fgij/fg.htm?mol=6sic FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sic OCA], [http://pdbe.org/6sic PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6sic RCSB], [http://www.ebi.ac.uk/pdbsum/6sic PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6sic 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=6sic FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sic OCA], [https://pdbe.org/6sic PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6sic RCSB], [https://www.ebi.ac.uk/pdbsum/6sic PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6sic ProSAT]</span></td></tr> |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
| |
| == Publication Abstract from PubMed ==
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| Cmr-beta is a type III-B CRISPR-Cas complex that, upon target RNA recognition, unleashes a multifaceted immune response against invading genetic elements, including single-stranded DNA (ssDNA) cleavage, cyclic oligoadenylate synthesis, and also a unique UA-specific single-stranded RNA (ssRNA) hydrolysis by the Cmr2 subunit. Here, we present the structure-function relationship of Cmr-beta, unveiling how binding of the target RNA regulates the Cmr2 activities. Cryoelectron microscopy (cryo-EM) analysis revealed the unique subunit architecture of Cmr-beta and captured the complex in different conformational stages of the immune response, including the non-cognate and cognate target-RNA-bound complexes. The binding of the target RNA induces a conformational change of Cmr2, which together with the complementation between the 5' tag in the CRISPR RNAs (crRNA) and the 3' antitag of the target RNA activate different configurations in a unique loop of the Cmr3 subunit, which acts as an allosteric sensor signaling the self- versus non-self-recognition. These findings highlight the diverse defense strategies of type III complexes.
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| Structures of the Cmr-beta Complex Reveal the Regulation of the Immunity Mechanism of Type III-B CRISPR-Cas.,Sofos N, Feng M, Stella S, Pape T, Fuglsang A, Lin J, Huang Q, Li Y, She Q, Montoya G Mol Cell. 2020 Jul 29. pii: S1097-2765(20)30474-3. doi:, 10.1016/j.molcel.2020.07.008. PMID:32730741<ref>PMID:32730741</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 6sic" style="background-color:#fffaf0;"></div>
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| == References ==
| |
| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Sulfolobus islandicus rey15a]]
| | [[Category: Montoya G]] |
| [[Category: Sulir]]
| | [[Category: Sofos N]] |
| [[Category: Montoya, G]] | | [[Category: Stella S]] |
| [[Category: Sofos, N]] | |
| [[Category: Stella, S]] | |
| [[Category: Antiviral protein]]
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| [[Category: Crispr-ca]]
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| [[Category: Cyclic oligo-adenylate synthase]]
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| [[Category: Effector complex]]
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| [[Category: Nuclease]]
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