7yhs: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7yhs]] is a 13 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=7YHS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YHS FirstGlance]. <br> | <table><tr><td colspan='2'>[[7yhs]] is a 13 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=7YHS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YHS FirstGlance]. <br> | ||
</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=7yhs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7yhs OCA], [https://pdbe.org/7yhs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7yhs RCSB], [https://www.ebi.ac.uk/pdbsum/7yhs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7yhs ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.37Å</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=7yhs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7yhs OCA], [https://pdbe.org/7yhs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7yhs RCSB], [https://www.ebi.ac.uk/pdbsum/7yhs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7yhs ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A3A8DDU9_PSEAI A0A3A8DDU9_PSEAI] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Latest revision as of 10:32, 3 July 2024
Structure of Csy-AcrIF4-dsDNAStructure of Csy-AcrIF4-dsDNA
Structural highlights
FunctionPublication Abstract from PubMedThe clustered regularly interspaced short palindromic repeats (CRISPR)-Cas system provides prokaryotes with protection against mobile genetic elements such as phages. In turn, phages deploy anti-CRISPR (Acr) proteins to evade this immunity. AcrIF4, an Acr targeting the type I-F CRISPR-Cas system, has been reported to bind the crRNA-guided surveillance (Csy) complex. However, it remains controversial whether AcrIF4 inhibits target DNA binding to the Csy complex. Here, we present structural and mechanistic studies into AcrIF4, exploring its unique anti-CRISPR mechanism. While the Csy-AcrIF4 complex displays decreased affinity for target DNA, it is still able to bind the DNA. Our structural and functional analyses of the Csy-AcrIF4-dsDNA complex revealed that AcrIF4 binding prevents rotation of the helical bundle of the Cas8f subunit induced by dsDNA binding, therefore resulting in failure of nuclease Cas2/3 recruitment and DNA cleavage. Overall, our study provides an interesting example of attack on the nuclease recruitment event by an Acr, but not conventional mechanisms of blocking binding of target DNA. Anti-CRISPR protein AcrIF4 inhibits the type I-F CRISPR-Cas surveillance complex by blocking nuclease recruitment and DNA cleavage.,Gao Z, Zhang L, Ge Z, Wang H, Yue Y, Jiang Z, Wang X, Xu C, Zhang Y, Yang M, Feng Y J Biol Chem. 2022 Nov;298(11):102575. doi: 10.1016/j.jbc.2022.102575. Epub 2022 , Oct 7. PMID:36209819[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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