6iuf: Difference between revisions

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<StructureSection load='6iuf' size='340' side='right'caption='[[6iuf]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
<StructureSection load='6iuf' size='340' side='right'caption='[[6iuf]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6iuf]] 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=6IUF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6IUF FirstGlance]. <br>
<table><tr><td colspan='2'>[[6iuf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Moraxella_bovoculi Moraxella bovoculi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IUF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6IUF FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.052&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AAX07_09540 ([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=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=6iuf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6iuf OCA], [http://pdbe.org/6iuf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6iuf RCSB], [http://www.ebi.ac.uk/pdbsum/6iuf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6iuf 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=6iuf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6iuf OCA], [https://pdbe.org/6iuf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6iuf RCSB], [https://www.ebi.ac.uk/pdbsum/6iuf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6iuf ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/A0A0U2B867_9GAMM A0A0U2B867_9GAMM]
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<ref>PMID:30936526</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6iuf" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc baa-1259]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Dong, L]]
[[Category: Moraxella bovoculi]]
[[Category: Guan, X]]
[[Category: Dong L]]
[[Category: Huang, Z]]
[[Category: Guan X]]
[[Category: Zhu, Y]]
[[Category: Huang Z]]
[[Category: Enzyme]]
[[Category: Zhu Y]]
[[Category: Immune system]]
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