6wc0: Difference between revisions

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-'''Unreleased structure'''
-The entry 6wc0 is ON HOLD  until Paper Publication
+==Crystal structure of AceCas9 bound with guide RNA and DNA with 5'-NNNTC-3' PAM==
+<StructureSection load='6wc0' size='340' side='right'caption='[[6wc0]], [[Resolution|resolution]] 3.61&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6wc0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Acidothermus_cellulolyticus_11B Acidothermus cellulolyticus 11B] 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=6WC0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6WC0 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]] 3.61&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</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=6wc0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wc0 OCA], [https://pdbe.org/6wc0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6wc0 RCSB], [https://www.ebi.ac.uk/pdbsum/6wc0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6wc0 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/A0LWB3_ACIC1 A0LWB3_ACIC1]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Acidothermus cellulolyticus CRISPR-Cas9 (AceCas9) is a thermophilic Type II-C enzyme that has potential genome editing applications in extreme environments. It cleaves DNA with a 5'-NNNCC-3' Protospacer Adjacent Motif (PAM) and is sensitive to its methylation status. To understand the molecular basis for the high specificity of AceCas9 for its PAM, we determined two crystal structures of AceCas9 lacking its HNH domain (AceCas9-DeltaHNH) bound with a single guide RNA and DNA substrates, one with the correct and the other with an incorrect PAM. Three residues, Glu1044, Arg1088, Arg1091, form an intricate hydrogen bond network with the first cytosine and the two opposing guanine nucleotides to confer specificity. Methylation of the first but not the second cytosine base abolishes AceCas9 activity, consistent with the observed PAM recognition pattern. The high sensitivity of AceCas9 to the modified cytosine makes it a potential device for detecting epigenomic changes in genomes.
-Authors:
+The molecular basis for recognition of 5'-NNNCC-3' PAM and its methylation state by Acidothermus cellulolyticus Cas9.,Das A, Hand TH, Smith CL, Wickline E, Zawrotny M, Li H Nat Commun. 2020 Dec 11;11(1):6346. doi: 10.1038/s41467-020-20204-1. PMID:33311465<ref>PMID:33311465</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6wc0" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Endonuclease 3D structures|Endonuclease 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Acidothermus cellulolyticus 11B]]
+[[Category: Large Structures]]
+[[Category: Synthetic construct]]
+[[Category: Das A]]
+[[Category: Li H]]