4qqy

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==Crystal structure of T. fusca Cas3-ADP==
==Crystal structure of T. fusca Cas3-ADP==
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<StructureSection load='4qqy' size='340' side='right' caption='[[4qqy]], [[Resolution|resolution]] 3.12&Aring;' scene=''>
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<StructureSection load='4qqy' size='340' side='right'caption='[[4qqy]], [[Resolution|resolution]] 3.12&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4qqy]] is a 8 chain structure. 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>
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<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>
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</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>
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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]] 3.12&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4qqw|4qqw]], [[4qqz|4qqz]]</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=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></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=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>
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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=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>
</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/Q47PJ0_THEFY Q47PJ0_THEFY]
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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&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 4qqy" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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*[[Endonuclease|Endonuclease]]
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*[[CRISPR type I-E (Cascade)|CRISPR type I-E (Cascade)]]
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*[[Helicase|Helicase]]
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*[[Endonuclease 3D structures|Endonuclease 3D structures]]
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== References ==
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*[[Helicase 3D structures|Helicase 3D structures]]
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Huo, Y]]
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[[Category: Large Structures]]
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[[Category: Ke, A]]
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[[Category: Thermobifida fusca YX]]
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[[Category: Nam, K H]]
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[[Category: Huo Y]]
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[[Category: Cas3]]
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[[Category: Ke A]]
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[[Category: Helicase]]
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[[Category: Nam KH]]
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[[Category: Hydrolase-dna complex]]
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[[Category: Rispr]]
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Current revision

Crystal structure of T. fusca Cas3-ADP

PDB ID 4qqy

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