6ox6: Difference between revisions
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<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=6ox6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ox6 OCA], [http://pdbe.org/6ox6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ox6 RCSB], [http://www.ebi.ac.uk/pdbsum/6ox6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ox6 ProSAT]</span></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=6ox6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ox6 OCA], [http://pdbe.org/6ox6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ox6 RCSB], [http://www.ebi.ac.uk/pdbsum/6ox6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ox6 ProSAT]</span></td></tr> | ||
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== 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> | |||
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<div class="pdbe-citations 6ox6" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
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</StructureSection> | </StructureSection> | ||
Revision as of 20:47, 20 November 2019
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
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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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