View source for 6epg


==Structure of the epsilon_1 / zeta_1 antitoxin / toxin system from Neisseria gonorrhoeae.==
<StructureSection load='6epg' size='340' side='right'caption='[[6epg]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6epg]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EPG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6EPG FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6epg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6epg OCA], [http://pdbe.org/6epg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6epg RCSB], [http://www.ebi.ac.uk/pdbsum/6epg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6epg ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bacterial toxin-antitoxin complexes are emerging as key players modulating bacterial physiology as activation of toxins induces stasis or programmed cell death by interference with vital cellular processes. Zeta toxins, which are prevalent in many bacterial genomes, were shown to interfere with cell wall formation by perturbing peptidoglycan synthesis in Gram-positive bacteria. Here, we characterize the epsilon/zeta toxin-antitoxin (TA) homologue from the Gram-negative pathogen Neisseria gonorrhoeae termed ng_varepsilon1 / ng_zeta1. Contrary to previously studied streptococcal epsilon/zeta TA systems, ng_varepsilon1 has an epsilon-unrelated fold and ng_zeta1 displays broader substrate specificity and phosphorylates multiple UDP-activated sugars that are precursors of peptidoglycan and lipopolysaccharide synthesis. Moreover, the phosphorylation site is different from the streptococcal zeta toxins, resulting in a different interference with cell wall synthesis. This difference most likely reflects adaptation to the individual cell wall composition of Gram-negative and Gram-positive organisms but also the distinct involvement of cell wall components in virulence.

The ng_zeta1 toxin of the gonococcal epsilon/zeta toxin/antitoxin system drains precursors for cell wall synthesis.,Rocker A, Peschke M, Kittila T, Sakson R, Brieke C, Meinhart A Nat Commun. 2018 Apr 27;9(1):1686. doi: 10.1038/s41467-018-03652-8. PMID:29703974<ref>PMID:29703974</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6epg" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Meinhart, A]]
[[Category: Rocker, A]]
[[Category: Antitoxin]]
[[Category: Bacterial toxin antitoxin system]]
[[Category: Small molecule kinase]]
[[Category: Toxin]]