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| | <SX load='6c66' size='340' side='right' viewer='molstar' caption='[[6c66]], [[Resolution|resolution]] 3.66Å' scene=''> | | <SX load='6c66' size='340' side='right' viewer='molstar' caption='[[6c66]], [[Resolution|resolution]] 3.66Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6c66]] is a 15 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Thefy Thefy]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6C66 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6C66 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6c66]] is a 15 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermobifida_fusca Thermobifida fusca] and [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=6C66 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6C66 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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">Electron Microscopy, [[Resolution|Resolution]] 3.66Å</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]), Tfu_1592 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=269800 THEFY]), Tfu_1590 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=269800 THEFY]), Tfu_1591 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=269800 THEFY]), Tfu_1589 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=269800 THEFY]), Tfu_1588 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=269800 THEFY])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[http://proteopedia.org/fgij/fg.htm?mol=6c66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6c66 OCA], [http://pdbe.org/6c66 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6c66 RCSB], [http://www.ebi.ac.uk/pdbsum/6c66 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6c66 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=6c66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6c66 OCA], [https://pdbe.org/6c66 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6c66 RCSB], [https://www.ebi.ac.uk/pdbsum/6c66 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6c66 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q47PJ0_THEFY Q47PJ0_THEFY] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </SX> | | </SX> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Thefy]] | + | [[Category: Thermobifida fusca]] |
| - | [[Category: Ke, A]] | + | [[Category: Thermobifida fusca YX]] |
| - | [[Category: Liao, M]] | + | [[Category: Ke A]] |
| - | [[Category: Luo, M]] | + | [[Category: Liao M]] |
| - | [[Category: Xiao, Y]] | + | [[Category: Luo M]] |
| - | [[Category: Cas3]]
| + | [[Category: Xiao Y]] |
| - | [[Category: Cascade]]
| + | |
| - | [[Category: Crispr-ca]]
| + | |
| - | [[Category: Dna binding protein]]
| + | |
| - | [[Category: Dna binding protein-dna-rna complex]]
| + | |
| Structural highlights
Function
Q47PJ0_THEFY
Publication Abstract from PubMed
Type I CRISPR-Cas system features a sequential target-searching and degradation process on double-stranded DNA, by the RNA-guided Cascade complex and the nuclease-helicase fusion enzyme Cas3, respectively. Here we present a 3.7 A resolution cryo-EM structure of the Type I-E Cascade/R-loop/Cas3 complex, poised to initiate DNA degradation. Cas3 distinguishes Cascade conformations and only captures the R-loop forming Cascade, to avoid cleaving partially complementary targets. Its nuclease domain recruits the non-target strand (NTS) DNA at a bulged region for the nicking of single-stranded DNA. An additional 4.7 A resolution cryo-EM structure captures the post-nicking state, in which the severed NTS retracts to the helicase entrance, to be threaded for ATP-dependent processive degradation. These snapshots form the basis for understanding RNA-guided DNA degradation in Type I-E CRISPR-Cas systems.
Structure basis for RNA-guided DNA degradation by Cascade and Cas3.,Xiao Y, Luo M, Dolan AE, Liao M, Ke A Science. 2018 Jun 7. pii: science.aat0839. doi: 10.1126/science.aat0839. PMID:29880725[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Xiao Y, Luo M, Dolan AE, Liao M, Ke A. Structure basis for RNA-guided DNA degradation by Cascade and Cas3. Science. 2018 Jun 7. pii: science.aat0839. doi: 10.1126/science.aat0839. PMID:29880725 doi:http://dx.doi.org/10.1126/science.aat0839
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