5id6: Difference between revisions
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<StructureSection load='5id6' size='340' side='right'caption='[[5id6]], [[Resolution|resolution]] 2.38Å' scene=''> | <StructureSection load='5id6' size='340' side='right'caption='[[5id6]], [[Resolution|resolution]] 2.38Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5id6]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5id6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lachnospiraceae_bacterium_ND2006 Lachnospiraceae bacterium ND2006] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ID6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ID6 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.382Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5id6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5id6 OCA], [https://pdbe.org/5id6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5id6 RCSB], [https://www.ebi.ac.uk/pdbsum/5id6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5id6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A182DWE3_9FIRM A0A182DWE3_9FIRM] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Lachnospiraceae bacterium | [[Category: Lachnospiraceae bacterium ND2006]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Dong | [[Category: Synthetic construct]] | ||
[[Category: Huang | [[Category: Dong D]] | ||
[[Category: Qiu | [[Category: Huang Z]] | ||
[[Category: Ren | [[Category: Qiu X]] | ||
[[Category: Wang | [[Category: Ren K]] | ||
[[Category: Wang J]] | |||
Latest revision as of 16:46, 30 August 2023
Structure of Cpf1/RNA ComplexStructure of Cpf1/RNA Complex
Structural highlights
FunctionPublication Abstract from PubMedThe CRISPR-Cas systems, as exemplified by CRISPR-Cas9, are RNA-guided adaptive immune systems used by bacteria and archaea to defend against viral infection. The CRISPR-Cpf1 system, a new class 2 CRISPR-Cas system, mediates robust DNA interference in human cells. Although functionally conserved, Cpf1 and Cas9 differ in many aspects including their guide RNAs and substrate specificity. Here we report the 2.38 A crystal structure of the CRISPR RNA (crRNA)-bound Lachnospiraceae bacterium ND2006 Cpf1 (LbCpf1). LbCpf1 has a triangle-shaped architecture with a large positively charged channel at the centre. Recognized by the oligonucleotide-binding domain of LbCpf1, the crRNA adopts a highly distorted conformation stabilized by extensive intramolecular interactions and the (Mg(H2O)6)(2+) ion. The oligonucleotide-binding domain also harbours a looped-out helical domain that is important for LbCpf1 substrate binding. Binding of crRNA or crRNA lacking the guide sequence induces marked conformational changes but no oligomerization of LbCpf1. Our study reveals the crRNA recognition mechanism and provides insight into crRNA-guided substrate binding of LbCpf1, establishing a framework for engineering LbCpf1 to improve its efficiency and specificity for genome editing. The crystal structure of Cpf1 in complex with CRISPR RNA.,Dong D, Ren K, Qiu X, Zheng J, Guo M, Guan X, Liu H, Li N, Zhang B, Yang D, Ma C, Wang S, Wu D, Ma Y, Fan S, Wang J, Gao N, Huang Z Nature. 2016 Apr 28;532(7600):522-6. doi: 10.1038/nature17944. Epub 2016 Apr 20. PMID:27096363[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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