7ae6
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
==Crystal structure of di-AMPylated HEPN(R102A) toxin== | ==Crystal structure of di-AMPylated HEPN(R102A) toxin== | ||
| - | <StructureSection load='7ae6' size='340' side='right'caption='[[7ae6]]' scene=''> | + | <StructureSection load='7ae6' size='340' side='right'caption='[[7ae6]], [[Resolution|resolution]] 1.65Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7AE6 OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[7ae6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aphanizomenon_flos-aquae_2012/KM1/D3 Aphanizomenon flos-aquae 2012/KM1/D3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7AE6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7AE6 FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=7ae6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ae6 OCA], [https://pdbe.org/7ae6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ae6 RCSB], [https://www.ebi.ac.uk/pdbsum/7ae6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ae6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/HEPT_APHF2 HEPT_APHF2] Toxic component of a type VII toxin-antitoxin (TA) system. Upon cloning in E.coli inhibits cell growth for several hours; eventually cells recover and start growing. Cleaves the last 4 nucleotides from the tRNA acceptor stem (shown in vitro with E.coli tRNA-Glu(UUC)); only cleaves intact tRNA. Has no activity on mRNA. Neutralized by coexpression with cognate antitoxin MntA, which is due to di-AMPylation of the RNase.<ref>PMID:33290744</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Prokaryotic toxin-antitoxin (TA) systems are composed of a toxin capable of interfering with key cellular processes and its neutralizing antidote, the antitoxin. Here, we focus on the HEPN-MNT TA system encoded in the vicinity of a subtype I-D CRISPR-Cas system in the cyanobacterium Aphanizomenon flos-aquae. We show that HEPN acts as a toxic RNase, which cleaves off 4 nt from the 3' end in a subset of tRNAs, thereby interfering with translation. Surprisingly, we find that the MNT (minimal nucleotidyltransferase) antitoxin inhibits HEPN RNase through covalent di-AMPylation (diadenylylation) of a conserved tyrosine residue, Y109, in the active site loop. Furthermore, we present crystallographic snapshots of the di-AMPylation reaction at different stages that explain the mechanism of HEPN RNase inactivation. Finally, we propose that the HEPN-MNT system functions as a cellular ATP sensor that monitors ATP homeostasis and, at low ATP levels, releases active HEPN toxin. | ||
| + | |||
| + | HEPN-MNT Toxin-Antitoxin System: The HEPN Ribonuclease Is Neutralized by OligoAMPylation.,Songailiene I, Juozapaitis J, Tamulaitiene G, Ruksenaite A, Sulcius S, Sasnauskas G, Venclovas C, Siksnys V Mol Cell. 2020 Dec 17;80(6):955-970.e7. doi: 10.1016/j.molcel.2020.11.034. Epub, 2020 Dec 7. PMID:33290744<ref>PMID:33290744</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7ae6" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Aphanizomenon flos-aquae 2012/KM1/D3]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Juozapaitis J]] | [[Category: Juozapaitis J]] | ||
Revision as of 12:07, 1 February 2024
Crystal structure of di-AMPylated HEPN(R102A) toxin
| |||||||||||
