View source for 7fa3


==Selenomethionine-derived structure of Aca1 in Pseudomonas phage JBD30==
<StructureSection load='7fa3' size='340' side='right'caption='[[7fa3]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7fa3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_phage_jbd30 Pseudomonas phage jbd30]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=7c0b 7c0b]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7FA3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7FA3 FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">JBD30_036 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1223260 Pseudomonas phage JBD30])</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=7fa3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7fa3 OCA], [https://pdbe.org/7fa3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7fa3 RCSB], [https://www.ebi.ac.uk/pdbsum/7fa3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7fa3 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
It has been shown that phages have evolved anti-CRISPR (Acr) proteins to inhibit host CRISPR-Cas systems. Most acr genes are located upstream of anti-CRISPR-associated (aca) genes, which is instrumental for identifying these acr genes. Thus far, eight Aca families (Aca1-Aca8) have been identified, all proteins of which share low sequence homology and bind to different target DNA sequences. Recently, Aca1 and Aca2 proteins were discovered to function as repressors by binding to acr-aca promoters, thus implying a potential anti-anti-CRISPR mechanism. However, the structural basis for the repression roles of Aca proteins is still unknown. Here, we elucidated apo-structures of Aca1 and Aca2 proteins and their complex structures with their cognate operator DNA in two model systems, the Pseudomonas phage JBD30 and the Pectobacterium carotovorum template phage ZF40. In combination with biochemical and cellular assays, our study unveils dimerization and DNA-recognition mechanisms of Aca1 and Aca2 family proteins, thus revealing the molecular basis for Aca1-and Aca2-mediated anti-CRISPR repression. Our results also shed light on understanding the repression roles of other Aca family proteins and autoregulation roles of acr-aca operons.

Structural basis for anti-CRISPR repression mediated by bacterial operon proteins Aca1 and Aca2.,Liu Y, Zhang L, Guo M, Chen L, Wu B, Huang H J Biol Chem. 2021 Dec;297(6):101357. doi: 10.1016/j.jbc.2021.101357. Epub 2021, Oct 28. PMID:34756887<ref>PMID:34756887</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7fa3" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas phage jbd30]]
[[Category: Huang, H]]
[[Category: Liu, Y]]
[[Category: Wu, B]]
[[Category: Zhang, L]]
[[Category: Anti-crispr]]
[[Category: Anti-crispr-associated]]
[[Category: Autoregulation]]
[[Category: Crispr]]
[[Category: Dna binding]]
[[Category: Transcription]]