6o6z

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Current revision (14:50, 13 March 2024) (edit) (undo)
 
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<StructureSection load='6o6z' size='340' side='right'caption='[[6o6z]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='6o6z' size='340' side='right'caption='[[6o6z]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6o6z]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6O6Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6O6Z FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6o6z]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermococcus_onnurineus_NA1 Thermococcus onnurineus NA1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6O6Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6O6Z FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LQJ:3-O-[(R)-{[(2S,3aS,4S,6S,6aS)-6-(6-amino-9H-purin-9-yl)-2-hydroxy-2-oxotetrahydro-2H-2lambda~5~-furo[3,4-d][1,3,2]dioxaphosphol-4-yl]methoxy}(hydroxy)phosphoryl]adenosine'>LQJ</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6o6z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o6z OCA], [http://pdbe.org/6o6z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6o6z RCSB], [http://www.ebi.ac.uk/pdbsum/6o6z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6o6z ProSAT]</span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LQJ:3-O-[(R)-{[(2S,3aS,4S,6S,6aS)-6-(6-amino-9H-purin-9-yl)-2-hydroxy-2-oxotetrahydro-2H-2lambda~5~-furo[3,4-d][1,3,2]dioxaphosphol-4-yl]methoxy}(hydroxy)phosphoryl]adenosine'>LQJ</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6o6z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o6z OCA], [https://pdbe.org/6o6z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6o6z RCSB], [https://www.ebi.ac.uk/pdbsum/6o6z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6o6z ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/B6YWC3_THEON B6YWC3_THEON]
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Type III-A CRISPR-Cas surveillance complexes containing multi-subunit Csm effector, guide, and target RNAs exhibit multiple activities, including formation of cyclic-oligoadenylates (cAn) from ATP and subsequent cAn-mediated cleavage of single-strand RNA (ssRNA) by the trans-acting Csm6 RNase. Our structure-function studies have focused on Thermococcus onnurineus Csm6 to deduce mechanistic insights into how cA4 binding to the Csm6 CARF domain triggers the RNase activity of the Csm6 HEPN domain and what factors contribute to regulation of RNA cleavage activity. We demonstrate that the Csm6 CARF domain is a ring nuclease, whereby bound cA4 is stepwise cleaved initially to ApApApA&gt;p and subsequently to ApA&gt;p in its CARF domain-binding pocket, with such cleavage bursts using a timer mechanism to regulate the RNase activity of the Csm6 HEPN domain. In addition, we establish T. onnurineus Csm6 as an adenosine-specific RNase and identify a histidine in the cA4 CARF-binding pocket involved in autoinhibitory regulation of RNase activity.
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CRISPR-Cas III-A Csm6 CARF Domain Is a Ring Nuclease Triggering Stepwise cA4 Cleavage with ApA&gt;p Formation Terminating RNase Activity.,Jia N, Jones R, Yang G, Ouerfelli O, Patel DJ Mol Cell. 2019 Jun 28. pii: S1097-2765(19)30447-2. doi:, 10.1016/j.molcel.2019.06.014. PMID:31326273<ref>PMID:31326273</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6o6z" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Jia, N]]
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[[Category: Thermococcus onnurineus NA1]]
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[[Category: Patel, D J]]
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[[Category: Jia N]]
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[[Category: Csm6]]
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[[Category: Patel DJ]]
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[[Category: Immune system]]
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[[Category: Type iii-a crispr-cas system]]
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Current revision

Crystal structure of Csm6 H381A in complex with cA4 by cocrystallization of cA4 and Csm6

PDB ID 6o6z

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