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| | ==Crystal structure of the anti-CRISPR protein, AcrIIA1== | | ==Crystal structure of the anti-CRISPR protein, AcrIIA1== |
| - | <StructureSection load='5y6a' size='340' side='right' caption='[[5y6a]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='5y6a' size='340' side='right'caption='[[5y6a]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5y6a]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Listeria_monocytogenes_j0161 Listeria monocytogenes j0161]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y6A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Y6A FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5y6a]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Listeria_monocytogenes_J0161 Listeria monocytogenes J0161]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y6A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5Y6A FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5y69|5y69]]</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]] 2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LMOG_03146 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=393130 Listeria monocytogenes J0161])</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=5y6a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y6a OCA], [https://pdbe.org/5y6a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5y6a RCSB], [https://www.ebi.ac.uk/pdbsum/5y6a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5y6a ProSAT]</span></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=5y6a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y6a OCA], [http://pdbe.org/5y6a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5y6a RCSB], [http://www.ebi.ac.uk/pdbsum/5y6a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5y6a ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A8ATW7_9CAUD A8ATW7_9CAUD] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Listeria monocytogenes j0161]] | + | [[Category: Large Structures]] |
| - | [[Category: An, S Y]] | + | [[Category: Listeria monocytogenes J0161]] |
| - | [[Category: Bae, E]] | + | [[Category: An SY]] |
| - | [[Category: Ka, D]] | + | [[Category: Bae E]] |
| - | [[Category: Suh, J Y]] | + | [[Category: Ka D]] |
| - | [[Category: Unknown function]]
| + | [[Category: Suh JY]] |
| - | [[Category: Viral protein]]
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| Structural highlights
Function
A8ATW7_9CAUD
Publication Abstract from PubMed
Clustered regularly interspaced short palindromic repeats (CRISPRs) and CRISPR-associated (Cas) proteins provide bacteria with RNA-based adaptive immunity against phage infection. To counteract this defense mechanism, phages evolved anti-CRISPR (Acr) proteins that inactivate the CRISPR-Cas systems. AcrIIA1, encoded by Listeria monocytogenes prophages, is the most prevalent among the Acr proteins targeting type II-A CRISPR-Cas systems and has been used as a marker to identify other Acr proteins. Here, we report the crystal structure of AcrIIA1 and its RNA-binding affinity. AcrIIA1 forms a dimer with a novel two helical-domain architecture. The N-terminal domain of AcrIIA1 exhibits a helix-turn-helix motif similar to transcriptional factors. When overexpressed in Escherichia coli, AcrIIA1 associates with RNAs, suggesting that AcrIIA1 functions via nucleic acid recognition. Taken together, the unique structural and functional features of AcrIIA1 suggest its distinct mode of Acr activity, expanding the diversity of the inhibitory mechanisms employed by Acr proteins.
Crystal structure of an anti-CRISPR protein, AcrIIA1.,Ka D, An SY, Suh JY, Bae E Nucleic Acids Res. 2017 Nov 22. pii: 4647678. doi: 10.1093/nar/gkx1181. PMID:29182776[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ka D, An SY, Suh JY, Bae E. Crystal structure of an anti-CRISPR protein, AcrIIA1. Nucleic Acids Res. 2017 Nov 22. pii: 4647678. doi: 10.1093/nar/gkx1181. PMID:29182776 doi:http://dx.doi.org/10.1093/nar/gkx1181
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