View source for 8d2n


==Structure of Acidothermus cellulolyticus Cas9 ternary complex (Pre-cleavage)==
<StructureSection load='8d2n' size='340' side='right'caption='[[8d2n]], [[Resolution|resolution]] 2.88&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8d2n]] 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=8D2N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8D2N FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.88&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=8d2n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8d2n OCA], [https://pdbe.org/8d2n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8d2n RCSB], [https://www.ebi.ac.uk/pdbsum/8d2n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8d2n ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0LWB3_ACIC1 A0LWB3_ACIC1] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Controlling the activity of the CRISPR-Cas9 system is essential to its safe adoption for clinical and research applications. Although the conformational dynamics of Cas9 are known to control its enzymatic activity, details of how Cas9 influences the catalytic processes at both nuclease domains remain elusive. Here we report five cryo-electron microscopy structures of the active Acidothermus cellulolyticus Cas9 complex along the reaction path at 2.2-2.9 A resolution. We observed that a large movement in one nuclease domain, triggered by the cognate DNA, results in noticeable changes in the active site of the other domain that is required for metal coordination and catalysis. Furthermore, the conformations synchronize the reaction intermediates, enabling coupled cutting of the two DNA strands. Consistent with the roles of conformations in organizing the active sites, adjustments to the metal-coordination residues lead to altered metal specificity of A. cellulolyticus Cas9 and commonly used Streptococcus pyogenes Cas9 in cells.

Coupled catalytic states and the role of metal coordination in Cas9.,Das A, Rai J, Roth MO, Shu Y, Medina ML, Barakat MR, Li H Nat Catal. 2023 Oct;6(10):969-977. doi: 10.1038/s41929-023-01031-1. Epub 2023 Oct , 2. PMID:38348449<ref>PMID:38348449</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8d2n" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Acidothermus cellulolyticus 11B]]
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Das A]]
[[Category: Li H]]
[[Category: Rai J]]