8rr6
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==MenT3 (aka TglT) toxin (Rv1045) from Mycobacterium tuberculosis H37Rv, non-phosphorylated== | |
| + | <StructureSection load='8rr6' size='340' side='right'caption='[[8rr6]], [[Resolution|resolution]] 1.78Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8rr6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8RR6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8RR6 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]] 1.78Å</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=8rr6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8rr6 OCA], [https://pdbe.org/8rr6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8rr6 RCSB], [https://www.ebi.ac.uk/pdbsum/8rr6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8rr6 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/P96356_MYCTU P96356_MYCTU] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Nucleotidyltransferases (NTases) control diverse physiological processes, including RNA modification, DNA replication and repair, and antibiotic resistance. The Mycobacterium tuberculosis NTase toxin family, MenT, modifies tRNAs to block translation. MenT toxin activity can be stringently regulated by diverse MenA antitoxins. There has been no unifying mechanism linking antitoxicity across MenT homologues. Here we demonstrate through structural, biochemical, biophysical and computational studies that despite lacking kinase motifs, antitoxin MenA(1) induces auto-phosphorylation of MenT(1) by repositioning the MenT(1) phosphoacceptor T39 active site residue towards bound nucleotide. Finally, we expand this predictive model to explain how unrelated antitoxin MenA(3) is similarly able to induce auto-phosphorylation of cognate toxin MenT(3). Our study reveals a conserved mechanism for the control of tuberculosis toxins, and demonstrates how active site auto-phosphorylation can regulate the activity of widespread NTases. | ||
| - | + | Inducible auto-phosphorylation regulates a widespread family of nucleotidyltransferase toxins.,Arrowsmith TJ, Xu X, Xu S, Usher B, Stokes P, Guest M, Bronowska AK, Genevaux P, Blower TR Nat Commun. 2024 Sep 4;15(1):7719. doi: 10.1038/s41467-024-51934-1. PMID:39231966<ref>PMID:39231966</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 8rr6" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mycobacterium tuberculosis H37Rv]] | ||
| + | [[Category: Arrowsmith TJ]] | ||
| + | [[Category: Blower TR]] | ||
Current revision
MenT3 (aka TglT) toxin (Rv1045) from Mycobacterium tuberculosis H37Rv, non-phosphorylated
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