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6as4

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Current revision (14:18, 13 March 2024) (edit) (undo)
 
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<StructureSection load='6as4' size='340' side='right'caption='[[6as4]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='6as4' size='340' side='right'caption='[[6as4]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6as4]] is a 3 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=6AS4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AS4 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6as4]] is a 3 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=6AS4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6AS4 FirstGlance]. <br>
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</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>
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</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&#8491;</td></tr>
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<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=6as4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6as4 OCA], [http://pdbe.org/6as4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6as4 RCSB], [http://www.ebi.ac.uk/pdbsum/6as4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6as4 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6as4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6as4 OCA], [https://pdbe.org/6as4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6as4 RCSB], [https://www.ebi.ac.uk/pdbsum/6as4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6as4 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/L7P7L6_9CAUD L7P7L6_9CAUD]
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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.
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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<ref>PMID:29233895</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6as4" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Pseudomonas phage jbd5]]
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[[Category: Pseudomonas phage JBD5]]
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[[Category: Calmettes, C]]
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[[Category: Calmettes C]]
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[[Category: Davidson, A R]]
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[[Category: Davidson AR]]
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[[Category: Maxwell, K L]]
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[[Category: Maxwell KL]]
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[[Category: Mejdani, M]]
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[[Category: Mejdani M]]
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[[Category: Moraes, T F]]
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[[Category: Moraes TF]]
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[[Category: Pawluk, A]]
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[[Category: Pawluk A]]
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[[Category: Shah, M]]
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[[Category: Shah M]]
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[[Category: Phage protein]]
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[[Category: Viral protein]]
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Current revision

Structure of a phage anti-CRISPR protein

PDB ID 6as4

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