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| | ==Cryo-EM structure of AcrVA5-acetylated MbCas12a in complex with crRNA== | | ==Cryo-EM structure of AcrVA5-acetylated MbCas12a in complex with crRNA== |
| - | <StructureSection load='6iv6' size='340' side='right'caption='[[6iv6]], [[Resolution|resolution]] 3.60Å' scene=''> | + | <SX load='6iv6' size='340' side='right' viewer='molstar' caption='[[6iv6]], [[Resolution|resolution]] 3.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6iv6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_baa-1259 Atcc baa-1259]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IV6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6IV6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6iv6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Moraxella_bovoculi Moraxella bovoculi] 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=6IV6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6IV6 FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.6Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AAX07_00205 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=386891 ATCC BAA-1259])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6iv6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6iv6 OCA], [http://pdbe.org/6iv6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6iv6 RCSB], [http://www.ebi.ac.uk/pdbsum/6iv6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6iv6 ProSAT]</span></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=6iv6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6iv6 OCA], [https://pdbe.org/6iv6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6iv6 RCSB], [https://www.ebi.ac.uk/pdbsum/6iv6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6iv6 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| - | </StructureSection> | + | </SX> |
| - | [[Category: Atcc baa-1259]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dong, L]] | + | [[Category: Moraxella bovoculi]] |
| - | [[Category: Gao, N]] | + | [[Category: Synthetic construct]] |
| - | [[Category: Guan, X]] | + | [[Category: Dong L]] |
| - | [[Category: Huang, Z]] | + | [[Category: Gao N]] |
| - | [[Category: Li, N]]
| + | [[Category: Guan X]] |
| - | [[Category: Zhu, Y]] | + | [[Category: Huang Z]] |
| - | [[Category: Enzyme]] | + | [[Category: Li N]] |
| - | [[Category: Immune system]] | + | [[Category: Zhu Y]] |
| - | [[Category: Immune system-rna complex]] | + | |
| Structural highlights
Publication Abstract from PubMed
Phages use anti-CRISPR proteins to deactivate the CRISPR-Cas system. The mechanisms for the inhibition of type I and type II systems by anti-CRISPRs have been elucidated. However, it has remained unknown how the type V CRISPR-Cas12a (Cpf1) system is inhibited by anti-CRISPRs. Here we identify the anti-CRISPR protein AcrVA5 and report the mechanisms by which it inhibits CRISPR-Cas12a. Our structural and biochemical data show that AcrVA5 functions as an acetyltransferase to modify Moraxella bovoculi (Mb) Cas12a at Lys635, a residue that is required for recognition of the protospacer-adjacent motif. The AcrVA5-mediated modification of MbCas12a results in complete loss of double-stranded DNA (dsDNA)-cleavage activity. In contrast, the Lys635Arg mutation renders MbCas12a completely insensitive to inhibition by AcrVA5. A cryo-EM structure of the AcrVA5-acetylated MbCas12a reveals that Lys635 acetylation provides sufficient steric hindrance to prevent dsDNA substrates from binding to the Cas protein. Our study reveals an unprecedented mechanism of CRISPR-Cas inhibition and suggests an evolutionary arms race between phages and bacteria.
An anti-CRISPR protein disables type V Cas12a by acetylation.,Dong L, Guan X, Li N, Zhang F, Zhu Y, Ren K, Yu L, Zhou F, Han Z, Gao N, Huang Z Nat Struct Mol Biol. 2019 Apr;26(4):308-314. doi: 10.1038/s41594-019-0206-1. Epub, 2019 Apr 1. PMID:30936526[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Dong L, Guan X, Li N, Zhang F, Zhu Y, Ren K, Yu L, Zhou F, Han Z, Gao N, Huang Z. An anti-CRISPR protein disables type V Cas12a by acetylation. Nat Struct Mol Biol. 2019 Apr;26(4):308-314. doi: 10.1038/s41594-019-0206-1. Epub, 2019 Apr 1. PMID:30936526 doi:http://dx.doi.org/10.1038/s41594-019-0206-1
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