6je3: Difference between revisions
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<StructureSection load='6je3' size='340' side='right'caption='[[6je3]], [[Resolution|resolution]] 2.93Å' scene=''> | <StructureSection load='6je3' size='340' side='right'caption='[[6je3]], [[Resolution|resolution]] 2.93Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6je3]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6je3]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis] 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=6JE3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JE3 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]] 2.931Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=6je3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6je3 OCA], [https://pdbe.org/6je3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6je3 RCSB], [https://www.ebi.ac.uk/pdbsum/6je3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6je3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</div> | </div> | ||
<div class="pdbe-citations 6je3" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6je3" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Endonuclease 3D structures|Endonuclease 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Cheng | [[Category: Neisseria meningitidis]] | ||
[[Category: Huang | [[Category: Synthetic construct]] | ||
[[Category: Liu | [[Category: Cheng Z]] | ||
[[Category: Sun | [[Category: Huang X]] | ||
[[Category: Wang | [[Category: Liu C]] | ||
[[Category: Wang | [[Category: Sun W]] | ||
[[Category: Yang | [[Category: Wang K]] | ||
[[Category: Wang Y]] | |||
[[Category: Yang J]] | |||
Latest revision as of 13:07, 22 November 2023
Crystal structure of Nme2Cas9 in complex with sgRNA and target DNA (AGGCCC PAM) with 5 nt overhangCrystal structure of Nme2Cas9 in complex with sgRNA and target DNA (AGGCCC PAM) with 5 nt overhang
Structural highlights
Publication Abstract from PubMedHigh-resolution Cas9 structures have yet to reveal catalytic conformations due to HNH nuclease domain positioning away from the cleavage site. Nme1Cas9 and Nme2Cas9 are compact nucleases for in vivo genome editing. Here, we report structures of meningococcal Cas9 homologs in complex with sgRNA, dsDNA, or the AcrIIC3 anti-CRISPR protein. DNA-bound structures represent an early step of target recognition, a later HNH pre-catalytic state, the HNH catalytic state, and a cleaved-target-DNA-bound state. In the HNH catalytic state of Nme1Cas9, the active site is seen poised at the scissile phosphodiester linkage of the target strand, providing a high-resolution view of the active conformation. The HNH active conformation activates the RuvC domain. Our structures explain how Nme1Cas9 and Nme2Cas9 read distinct PAM sequences and how AcrIIC3 inhibits Nme1Cas9 activity. These structures provide insights into Cas9 domain rearrangements, guide-target engagement, cleavage mechanism, and anti-CRISPR inhibition, facilitating the optimization of these genome-editing platforms. Structures of Neisseria meningitidis Cas9 Complexes in Catalytically Poised and Anti-CRISPR-Inhibited States.,Sun W, Yang J, Cheng Z, Amrani N, Liu C, Wang K, Ibraheim R, Edraki A, Huang X, Wang M, Wang J, Liu L, Sheng G, Yang Y, Lou J, Sontheimer EJ, Wang Y Mol Cell. 2019 Oct 22. pii: S1097-2765(19)30730-0. doi:, 10.1016/j.molcel.2019.09.025. PMID:31668930[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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