View source for 7zge


==BrxA, BREX phage defence protein==
<StructureSection load='7zge' size='340' side='right'caption='[[7zge]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7zge]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_fergusonii_ATCC_35469 Escherichia fergusonii ATCC 35469]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ZGE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ZGE FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.09&#8491;</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=7zge FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7zge OCA], [https://pdbe.org/7zge PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7zge RCSB], [https://www.ebi.ac.uk/pdbsum/7zge PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7zge ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B7L3Y4_ESCF3 B7L3Y4_ESCF3] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bacteria use adaptive CRISPR-Cas immune mechanisms to protect from invasion by bacteriophages and other mobile genetic elements. In response, bacteriophages and mobile genetic elements have co-evolved anti-CRISPR proteins to inhibit the bacterial defense. We and others have previously shown that anti-CRISPR associated (Aca) proteins can regulate this anti-CRISPR counter-attack. Here, we report the first structure of an Aca protein, the Aca2 DNA-binding transcriptional autorepressor from Pectobacterium carotovorum bacteriophage ZF40, determined to 1.34 A. Aca2 presents a conserved N-terminal helix-turn-helix DNA-binding domain and a previously uncharacterized C-terminal dimerization domain. Dimerization positions the Aca2 recognition helices for insertion into the major grooves of target DNA, supporting its role in regulating anti-CRISPRs. Furthermore, database comparisons identified uncharacterized Aca2 structural homologs in pathogenic bacteria, suggesting that Aca2 represents the first characterized member of a more widespread family of transcriptional regulators.

Crystal structure of the anti-CRISPR repressor Aca2.,Usher B, Birkholz N, Beck IN, Fagerlund RD, Jackson SA, Fineran PC, Blower TR J Struct Biol. 2021 Jun 8;213(3):107752. doi: 10.1016/j.jsb.2021.107752. PMID:34116143<ref>PMID:34116143</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7zge" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia fergusonii ATCC 35469]]
[[Category: Large Structures]]
[[Category: Beck IN]]
[[Category: Blower TR]]
[[Category: Picton DM]]