View source for 5cze


==Crystal structure of the PaaA2-ParE2 antitoxin-toxin complex==
<StructureSection load='5cze' size='340' side='right'caption='[[5cze]], [[Resolution|resolution]] 3.82&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5cze]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7_str._SS52 Escherichia coli O157:H7 str. SS52]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CZE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CZE 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]] 3.82&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=5cze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cze OCA], [https://pdbe.org/5cze PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cze RCSB], [https://www.ebi.ac.uk/pdbsum/5cze PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cze ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0D7C2L1_ECOLX A0A0D7C2L1_ECOLX] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Many bacterial pathogens modulate their metabolic activity, virulence and pathogenicity through so-called "toxin-antitoxin" (TA) modules. The genome of the human pathogen Escherichia coli O157 contains two three-component TA modules related to the known parDE module. Here, we show that the toxin EcParE2 maps in a branch of the RelE/ParE toxin superfamily that is distinct from the branches that contain verified gyrase and ribosome inhibitors. The structure of EcParE2 closely resembles that of Caulobacter crescentus ParE but shows a distinct pattern of conserved surface residues, in agreement with its apparent inability to interact with GyrA. The antitoxin EcPaaA2 is characterized by two alpha-helices (H1 and H2) that serve as molecular recognition elements to wrap itself around EcParE2. Both EcPaaA2 H1 and H2 are required to sustain a high-affinity interaction with EcParE2 and for the inhibition of EcParE2-mediated killing in vivo. Furthermore, evidence demonstrates that EcPaaA2 H2, but not H1, determines specificity for EcParE2. The initially formed EcPaaA2-EcParE2 heterodimer then assembles into a hetero-hexadecamer, which is stable in solution and is formed in a highly cooperative manner. Together these findings provide novel data on quaternary structure, TA interactions and activity of a hitherto poorly characterized family of TA modules.

A unique hetero-hexadecameric architecture displayed by the Escherichia coli O157 PaaA2-ParE2 antitoxin-toxin complex.,Sterckx YG, Jove T, Shkumatov AV, Garcia-Pino A, Geerts L, De Kerpel M, Lah J, De Greve H, Van Melderen L, Loris R J Mol Biol. 2016 Apr 24;428(8):1589-603. doi: 10.1016/j.jmb.2016.03.007. Epub, 2016 Mar 18. PMID:26996937<ref>PMID:26996937</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5cze" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Escherichia coli O157:H7 str. SS52]]
[[Category: Large Structures]]
[[Category: Loris R]]
[[Category: Sterckx YGJ]]