View source for 7chd


==AtaT complexed with acetyl-methionyl-tRNAfMet==
<StructureSection load='7chd' size='340' side='right'caption='[[7chd]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7chd]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CHD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CHD 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]] 3.804&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4SU:4-THIOURIDINE-5-MONOPHOSPHATE'>4SU</scene>, <scene name='pdbligand=5MU:5-METHYLURIDINE+5-MONOPHOSPHATE'>5MU</scene>, <scene name='pdbligand=H2U:5,6-DIHYDROURIDINE-5-MONOPHOSPHATE'>H2U</scene>, <scene name='pdbligand=OMC:O2-METHYLYCYTIDINE-5-MONOPHOSPHATE'>OMC</scene>, <scene name='pdbligand=PSU:PSEUDOURIDINE-5-MONOPHOSPHATE'>PSU</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=7chd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7chd OCA], [https://pdbe.org/7chd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7chd RCSB], [https://www.ebi.ac.uk/pdbsum/7chd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7chd ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8XED1_ECO57 Q8XED1_ECO57] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Toxin-antitoxin systems in bacteria contribute to stress adaptation, dormancy, and persistence. AtaT, a type-II toxin in enterohemorrhagic E. coli, reportedly acetylates the alpha-amino group of the aminoacyl-moiety of initiator Met-tRNAf(Met), thus inhibiting translation initiation. Here, we show that AtaT has a broader specificity for aminoacyl-tRNAs than initially claimed. AtaT efficiently acetylates Gly-tRNA(Gly), Trp-tRNA(Trp), Tyr-tRNA(Tyr) and Phe-tRNA(Phe) isoacceptors, in addition to Met-tRNAf(Met), and inhibits global translation. AtaT interacts with the acceptor stem of tRNAf(Met), and the consecutive G-C pairs in the bottom-half of the acceptor stem are required for acetylation. Consistently, tRNA(Gly), tRNA(Trp), tRNA(Tyr) and tRNA(Phe) also possess consecutive G-C base-pairs in the bottom halves of their acceptor stems. Furthermore, misaminoacylated valyl-tRNAf(Met) and isoleucyl-tRNAf(Met) are not acetylated by AtaT. Therefore, the substrate selection by AtaT is governed by the specific acceptor stem sequence and the properties of the aminoacyl-moiety of aminoacyl-tRNAs.

Mechanism of aminoacyl-tRNA acetylation by an aminoacyl-tRNA acetyltransferase AtaT from enterohemorrhagic E. coli.,Yashiro Y, Sakaguchi Y, Suzuki T, Tomita K Nat Commun. 2020 Oct 28;11(1):5438. doi: 10.1038/s41467-020-19281-z. PMID:33116145<ref>PMID:33116145</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7chd" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli O157:H7]]
[[Category: Large Structures]]
[[Category: Tomita K]]
[[Category: Yashiro Y]]