6ox6: Difference between revisions
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The | ==Crystal structure of the complex between the Type VI effector Tas1 and its immunity protein== | ||
<StructureSection load='6ox6' size='340' side='right'caption='[[6ox6]], [[Resolution|resolution]] 2.17Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6ox6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OX6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OX6 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]] 2.17Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <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'>[https://proteopedia.org/fgij/fg.htm?mol=6ox6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ox6 OCA], [https://pdbe.org/6ox6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ox6 RCSB], [https://www.ebi.ac.uk/pdbsum/6ox6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ox6 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/TSE6_PSEAE TSE6_PSEAE] Type VI secretion exported toxin that acts as a glycohydrolase on bacterial target cells and degrades the essential dinucleotides NAD(+) and NADP(+), thereby inducing bacteriostasis. The activity resides in the C-terminal region that is initially neutralized by the cognate immunity protein Tsi6.<ref>PMID:26456113</ref> <ref>PMID:30177742</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Bacteria have evolved sophisticated mechanisms to inhibit the growth of competitors(1). One such mechanism involves type VI secretion systems, which bacteria can use to inject antibacterial toxins directly into neighbouring cells. Many of these toxins target the integrity of the cell envelope, but the full range of growth inhibitory mechanisms remains unknown(2). Here we identify a type VI secretion effector, Tas1, in the opportunistic pathogen Pseudomonas aeruginosa. The crystal structure of Tas1 shows that it is similar to enzymes that synthesize (p)ppGpp, a broadly conserved signalling molecule in bacteria that modulates cell growth rate, particularly in response to nutritional stress(3). However, Tas1 does not synthesize (p)ppGpp; instead, it pyrophosphorylates adenosine nucleotides to produce (p)ppApp at rates of nearly 180,000 molecules per minute. Consequently, the delivery of Tas1 into competitor cells drives rapid accumulation of (p)ppApp, depletion of ATP, and widespread dysregulation of essential metabolic pathways, thereby resulting in target cell death. Our findings reveal a previously undescribed mechanism for interbacterial antagonism and demonstrate a physiological role for the metabolite (p)ppApp in bacteria. | |||
An interbacterial toxin inhibits target cell growth by synthesizing (p)ppApp.,Ahmad S, Wang B, Walker MD, Tran HR, Stogios PJ, Savchenko A, Grant RA, McArthur AG, Laub MT, Whitney JC Nature. 2019 Nov 6. pii: 10.1038/s41586-019-1735-9. doi:, 10.1038/s41586-019-1735-9. PMID:31695193<ref>PMID:31695193</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6ox6" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Pseudomonas aeruginosa]] | |||
[[Category: Ahmad S]] | |||
[[Category: Joachimiak A]] | |||
[[Category: Satchell KJF]] | |||
[[Category: Savchenko A]] | |||
[[Category: Skarina T]] | |||
[[Category: Stogios PJ]] | |||
[[Category: Whitney J]] | |||
Latest revision as of 14:15, 30 October 2024
Crystal structure of the complex between the Type VI effector Tas1 and its immunity proteinCrystal structure of the complex between the Type VI effector Tas1 and its immunity protein
Structural highlights
FunctionTSE6_PSEAE Type VI secretion exported toxin that acts as a glycohydrolase on bacterial target cells and degrades the essential dinucleotides NAD(+) and NADP(+), thereby inducing bacteriostasis. The activity resides in the C-terminal region that is initially neutralized by the cognate immunity protein Tsi6.[1] [2] Publication Abstract from PubMedBacteria have evolved sophisticated mechanisms to inhibit the growth of competitors(1). One such mechanism involves type VI secretion systems, which bacteria can use to inject antibacterial toxins directly into neighbouring cells. Many of these toxins target the integrity of the cell envelope, but the full range of growth inhibitory mechanisms remains unknown(2). Here we identify a type VI secretion effector, Tas1, in the opportunistic pathogen Pseudomonas aeruginosa. The crystal structure of Tas1 shows that it is similar to enzymes that synthesize (p)ppGpp, a broadly conserved signalling molecule in bacteria that modulates cell growth rate, particularly in response to nutritional stress(3). However, Tas1 does not synthesize (p)ppGpp; instead, it pyrophosphorylates adenosine nucleotides to produce (p)ppApp at rates of nearly 180,000 molecules per minute. Consequently, the delivery of Tas1 into competitor cells drives rapid accumulation of (p)ppApp, depletion of ATP, and widespread dysregulation of essential metabolic pathways, thereby resulting in target cell death. Our findings reveal a previously undescribed mechanism for interbacterial antagonism and demonstrate a physiological role for the metabolite (p)ppApp in bacteria. An interbacterial toxin inhibits target cell growth by synthesizing (p)ppApp.,Ahmad S, Wang B, Walker MD, Tran HR, Stogios PJ, Savchenko A, Grant RA, McArthur AG, Laub MT, Whitney JC Nature. 2019 Nov 6. pii: 10.1038/s41586-019-1735-9. doi:, 10.1038/s41586-019-1735-9. PMID:31695193[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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