4qqx: Difference between revisions
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==Crystal structure of T. fusca Cas3-ATP== | |||
<StructureSection load='4qqx' size='340' side='right'caption='[[4qqx]], [[Resolution|resolution]] 3.34Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4qqx]] 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=4QQX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QQX FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.34Å</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=FE:FE+(III)+ION'>FE</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=4qqx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qqx OCA], [https://pdbe.org/4qqx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qqx RCSB], [https://www.ebi.ac.uk/pdbsum/4qqx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qqx ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q47PJ0_THEFY Q47PJ0_THEFY] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4qqx" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[CRISPR type I-E (Cascade)|CRISPR type I-E (Cascade)]] | |||
*[[Endonuclease 3D structures|Endonuclease 3D structures]] | |||
*[[Helicase 3D structures|Helicase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Thermobifida fusca YX]] | |||
[[Category: Huo Y]] | |||
[[Category: Ke A]] | |||
[[Category: Nam KH]] | |||
