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| <StructureSection load='4qqy' size='340' side='right'caption='[[4qqy]], [[Resolution|resolution]] 3.12Å' scene=''> | | <StructureSection load='4qqy' size='340' side='right'caption='[[4qqy]], [[Resolution|resolution]] 3.12Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[4qqy]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Thefy Thefy]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QQY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QQY FirstGlance]. <br> | | <table><tr><td colspan='2'>[[4qqy]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermobifida_fusca_YX Thermobifida fusca YX]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QQY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QQY FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.12Å</td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4qqw|4qqw]], [[4qqz|4qqz]]</td></tr> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Tfu_1593 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=269800 THEFY])</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=4qqy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qqy OCA], [https://pdbe.org/4qqy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qqy RCSB], [https://www.ebi.ac.uk/pdbsum/4qqy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qqy ProSAT]</span></td></tr> |
| <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=4qqy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qqy OCA], [http://pdbe.org/4qqy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qqy RCSB], [http://www.ebi.ac.uk/pdbsum/4qqy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qqy ProSAT]</span></td></tr> | |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
| | == Function == |
| == Publication Abstract from PubMed == | | [https://www.uniprot.org/uniprot/Q47PJ0_THEFY Q47PJ0_THEFY] |
| CRISPR drives prokaryotic adaptation to invasive nucleic acids such as phages and plasmids, using an RNA-mediated interference mechanism. Interference in type I CRISPR-Cas systems requires a targeting Cascade complex and a degradation machine, Cas3, which contains both nuclease and helicase activities. Here we report the crystal structures of Thermobifida fusca Cas3 bound to single-stranded (ss) DNA substrate and show that it is an obligate 3'-to-5' ssDNase that preferentially accepts substrate directly from the helicase moiety. Conserved residues in the HD-type nuclease coordinate two irons for ssDNA cleavage. We demonstrate ATP coordination and conformational flexibility of the SF2-type helicase domain. Cas3 is specifically guided toward Cascade-bound target DNA by a PAM sequence, through physical interactions with both the nontarget substrate strand and the CasA protein. The sequence of recognition events ensures well-controlled DNA targeting and degradation of foreign DNA by Cascade and Cas3.
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| Structures of CRISPR Cas3 offer mechanistic insights into Cascade-activated DNA unwinding and degradation.,Huo Y, Nam KH, Ding F, Lee H, Wu L, Xiao Y, Farchione MD Jr, Zhou S, Rajashankar K, Kurinov I, Zhang R, Ke A Nat Struct Mol Biol. 2014 Aug 17. doi: 10.1038/nsmb.2875. PMID:25132177<ref>PMID:25132177</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 4qqy" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[CRISPR type I-E (Cascade)|CRISPR type I-E (Cascade)]] | | *[[CRISPR type I-E (Cascade)|CRISPR type I-E (Cascade)]] |
| *[[Endonuclease|Endonuclease]] | | *[[Endonuclease 3D structures|Endonuclease 3D structures]] |
| *[[Helicase|Helicase]] | | *[[Helicase 3D structures|Helicase 3D structures]] |
| == References ==
| |
| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Thefy]] | | [[Category: Thermobifida fusca YX]] |
| [[Category: Huo, Y]] | | [[Category: Huo Y]] |
| [[Category: Ke, A]] | | [[Category: Ke A]] |
| [[Category: Nam, K H]] | | [[Category: Nam KH]] |
| [[Category: Cas3]]
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| [[Category: Helicase]]
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| [[Category: Hydrolase-dna complex]]
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| [[Category: Rispr]]
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