5xn4: Difference between revisions
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==Anti-CRISPR protein AcrIIA4== | |||
<StructureSection load='5xn4' size='340' side='right'caption='[[5xn4]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5xn4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XN4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XN4 FirstGlance]. <br> | |||
</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=5xn4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xn4 OCA], [https://pdbe.org/5xn4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xn4 RCSB], [https://www.ebi.ac.uk/pdbsum/5xn4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xn4 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A247D711_LISMN A0A247D711_LISMN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The bacterial CRISPR-Cas system provides adaptive immunity against invading phages. Cas9, an RNA-guided endonuclease, specifically cleaves target DNA substrates and constitutes a well-established platform for genome editing. Recently, anti-CRISPR (Acr) proteins that inhibit Cas9 have been discovered, promising a useful off-switch for Cas9 to avoid undesirable off-target effects. Here, we report the solution structure and dynamics of Listeria monocytogenes AcrIIA4 that inhibits Streptococcus pyogenes Cas9 (SpyCas9). AcrIIA4 forms a compact monomeric alphabetabetabetaalphaalpha fold comprising three antiparallel beta strands flanked by three alpha-helices and a short 310-helix. AcrIIA4 exhibits distinct backbone dynamics in fast and slow timescales at loop regions that form interaction surfaces for SpyCas9. In particular, the beta1-beta2 loop that binds to the RuvC domain of SpyCas9 is highly mobile, and the beta1-beta2 and alpha2-alpha3 loops that bind to the RuvC and C-terminal domains of SpyCas9, respectively, undergoes conformational exchanges in microsecond-to-millisecond time scales. AcrIIA4 binds to apo-SpyCas9 with KD ~4.8 muM, which compares to KD ~0.6 nM for AcrIIA4 binding to sgRNA-bound SpyCas9. Since the binary complex between AcrIIA4 and SpyCas9 does not compete with the target DNA binding, it can effectively disable the Cas9 nuclease activity by forming a tight ternary complex in the presence of sgRNA. | |||
Solution structure and dynamics of anti-CRISPR AcrIIA4, the Cas9 inhibitor.,Kim I, Jeong M, Ka D, Han M, Kim NK, Bae E, Suh JY Sci Rep. 2018 Mar 1;8(1):3883. doi: 10.1038/s41598-018-22177-0. PMID:29497118<ref>PMID:29497118</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5xn4" style="background-color:#fffaf0;"></div> | ||
[[Category: Kim | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Listeria monocytogenes]] | |||
[[Category: Kim I]] | |||
[[Category: Suh J-Y]] | |||
Latest revision as of 10:30, 14 June 2023
Anti-CRISPR protein AcrIIA4
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