View source for 6gtq


==Structure of the AtaT Y144F mutant toxin bound to the C-terminus of the antitoxin AtaR==
<StructureSection load='6gtq' size='340' side='right'  caption='[[6gtq]], [[Resolution|resolution]] 2.49&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6gtq]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GTQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GTQ FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6gtq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gtq OCA], [http://pdbe.org/6gtq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gtq RCSB], [http://www.ebi.ac.uk/pdbsum/6gtq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gtq ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
GCN5-related N-acetyl-transferase (GNAT)-like enzymes from toxin-antitoxin modules are strong inhibitors of protein synthesis. Here, we present the bases of the regulatory mechanisms of ataRT, a model GNAT-toxin-antitoxin module, from toxin synthesis to its action as a transcriptional de-repressor. We show the antitoxin (AtaR) traps the toxin (AtaT) in a pre-catalytic monomeric state and precludes the effective binding of ac-CoA and its target Met-transfer RNA(fMet). In the repressor complex, AtaR intrinsically disordered region interacts with AtaT at two different sites, folding into different structures, that are involved in two separate functional roles, toxin neutralization and placing the DNA-binding domains of AtaR in a binding-compatible orientation. Our data suggests AtaR neutralizes AtaT as a monomer, right after its synthesis and only the toxin-antitoxin complex formed in this way is an active repressor. Once activated by dimerization, later neutralization of the toxin results in a toxin-antitoxin complex that is not able to repress transcription.

Mechanism of regulation and neutralization of the AtaR-AtaT toxin-antitoxin system.,Jurenas D, Van Melderen L, Garcia-Pino A Nat Chem Biol. 2019 Mar;15(3):285-294. doi: 10.1038/s41589-018-0216-z. Epub 2019 , Feb 4. PMID:30718814<ref>PMID:30718814</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6gtq" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Garcia-Pino, A]]
[[Category: Jurenas, D]]
[[Category: Antitoxin]]
[[Category: Bacterial repressor]]
[[Category: N-acetyl transferase]]
[[Category: Rhh]]
[[Category: Ribbon-helix-helix]]
[[Category: Ta toxin]]
[[Category: Toxin-antitoxin complex]]
[[Category: Transcription]]