6kyf: Difference between revisions

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<StructureSection load='6kyf' size='340' side='right'caption='[[6kyf]], [[Resolution|resolution]] 3.07&Aring;' scene=''>
<StructureSection load='6kyf' size='340' side='right'caption='[[6kyf]], [[Resolution|resolution]] 3.07&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6kyf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KYF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KYF FirstGlance]. <br>
<table><tr><td colspan='2'>[[6kyf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KYF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KYF FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</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]] 3.07&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NCTC11440_04410 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</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=6kyf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kyf OCA], [https://pdbe.org/6kyf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6kyf RCSB], [https://www.ebi.ac.uk/pdbsum/6kyf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6kyf 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=6kyf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kyf OCA], [https://pdbe.org/6kyf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6kyf RCSB], [https://www.ebi.ac.uk/pdbsum/6kyf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6kyf ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
CRISPR-Cas systems are bacterial anti-viral systems, and phages use anti-CRISPR proteins (Acrs) to inactivate these systems. Here, we report a novel mechanism by which AcrIF11 inhibits the type I-F CRISPR system. Our structural and biochemical studies demonstrate that AcrIF11 functions as a novel mono-ADP-ribosyltransferase (mART) to modify N250 of the Cas8f subunit, a residue required for recognition of the protospacer-adjacent motif, within the crRNA-guided surveillance (Csy) complex from Pseudomonas aeruginosa. The AcrIF11-mediated ADP-ribosylation of the Csy complex results in complete loss of its double-stranded DNA (dsDNA) binding activity. Biochemical studies show that AcrIF11 requires, besides Cas8f, the Cas7.6f subunit for binding to and modifying the Csy complex. Our study not only reveals an unprecedented mechanism of type I CRISPR-Cas inhibition and the evolutionary arms race between phages and bacteria but also suggests an approach for designing highly potent regulatory tools in the future applications of type I CRISPR-Cas systems.
A Type I-F Anti-CRISPR Protein Inhibits the CRISPR-Cas Surveillance Complex by ADP-Ribosylation.,Niu Y, Yang L, Gao T, Dong C, Zhang B, Yin P, Hopp AK, Li D, Gan R, Wang H, Liu X, Cao X, Xie Y, Meng X, Deng H, Zhang X, Ren J, Hottiger MO, Chen Z, Zhang Y, Liu X, Feng Y Mol Cell. 2020 Nov 5;80(3):512-524.e5. doi: 10.1016/j.molcel.2020.09.015. Epub, 2020 Oct 12. PMID:33049228<ref>PMID:33049228</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6kyf" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Feng, Y]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Niu, Y]]
[[Category: Feng Y]]
[[Category: Wang, H]]
[[Category: Niu Y]]
[[Category: Zhang, Y]]
[[Category: Wang H]]
[[Category: Enzyme]]
[[Category: Zhang Y]]
[[Category: Nad]]
[[Category: Viral protein]]

Latest revision as of 10:44, 27 March 2024

Crystal structure of an anti-CRISPR protein

6kyf, resolution 3.07Å

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