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| | <StructureSection load='6as3' size='340' side='right'caption='[[6as3]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='6as3' size='340' side='right'caption='[[6as3]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6as3]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_phage_jbd5 Pseudomonas phage jbd5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AS3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AS3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6as3]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_phage_JBD5 Pseudomonas phage JBD5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AS3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6AS3 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">JBD5_034 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1223261 Pseudomonas phage JBD5])</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='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=6as3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6as3 OCA], [http://pdbe.org/6as3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6as3 RCSB], [http://www.ebi.ac.uk/pdbsum/6as3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6as3 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=6as3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6as3 OCA], [https://pdbe.org/6as3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6as3 RCSB], [https://www.ebi.ac.uk/pdbsum/6as3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6as3 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/L7P7L6_9CAUD L7P7L6_9CAUD] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pseudomonas phage jbd5]] | + | [[Category: Pseudomonas phage JBD5]] |
| - | [[Category: Calmettes, C]] | + | [[Category: Calmettes C]] |
| - | [[Category: Davidson, A R]] | + | [[Category: Davidson AR]] |
| - | [[Category: Maxwell, K L]] | + | [[Category: Maxwell KL]] |
| - | [[Category: Mejdani, M]] | + | [[Category: Mejdani M]] |
| - | [[Category: Moraes, T F]] | + | [[Category: Moraes TF]] |
| - | [[Category: Pawluk, A]] | + | [[Category: Pawluk A]] |
| - | [[Category: Shah, M]] | + | [[Category: Shah M]] |
| - | [[Category: Phage protein]]
| + | |
| - | [[Category: Unknown function]]
| + | |
| Structural highlights
Function
L7P7L6_9CAUD
Publication Abstract from PubMed
CRISPR (clustered regularly interspaced short palindromic repeat)-Cas adaptive immune systems are prevalent defense mechanisms in bacteria and archaea. They provide sequence-specific detection and neutralization of foreign nucleic acids such as bacteriophages and plasmids. One mechanism by which phages and other mobile genetic elements are able to overcome the CRISPR-Cas system is through the expression of anti-CRISPR proteins. Over 20 different families of anti-CRISPR proteins have been described, each of which inhibits a particular type of CRISPR-Cas system. In this work, we determined the structure of type I-E anti-CRISPR protein AcrE1 by X-ray crystallography. We show that AcrE1 binds to the CRISPR-associated helicase/nuclease Cas3 and that the C-terminal region of the anti-CRISPR protein is important for its inhibitory activity. We further show that AcrE1 can convert the endogenous type I-E CRISPR system into a programmable transcriptional repressor.IMPORTANCE The CRISPR-Cas immune system provides bacteria with resistance to invasion by potentially harmful viruses, plasmids, and other foreign mobile genetic elements. This study presents the first structural and mechanistic insight into a phage-encoded protein that inactivates the type I-E CRISPR-Cas system in Pseudomonas aeruginosa The interaction of this anti-CRISPR protein with the CRISPR-associated helicase/nuclease proteins Cas3 shuts down the CRISPR-Cas system and protects phages carrying this gene from destruction. This interaction also allows the repurposing of the endogenous type I-E CRISPR system into a programmable transcriptional repressor, providing a new biotechnological tool for genetic studies of bacteria encoding this type I-E CRISPR-Cas system.
Disabling a Type I-E CRISPR-Cas Nuclease with a Bacteriophage-Encoded Anti-CRISPR Protein.,Pawluk A, Shah M, Mejdani M, Calmettes C, Moraes TF, Davidson AR, Maxwell KL MBio. 2017 Dec 12;8(6). pii: mBio.01751-17. doi: 10.1128/mBio.01751-17. PMID:29233895[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Pawluk A, Shah M, Mejdani M, Calmettes C, Moraes TF, Davidson AR, Maxwell KL. Disabling a Type I-E CRISPR-Cas Nuclease with a Bacteriophage-Encoded Anti-CRISPR Protein. MBio. 2017 Dec 12;8(6). pii: mBio.01751-17. doi: 10.1128/mBio.01751-17. PMID:29233895 doi:http://dx.doi.org/10.1128/mBio.01751-17
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