6eph: Difference between revisions
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==Structure of the epsilon_1 / zeta_1 antitoxin toxin system from Neisseria gonorrhoeae in complex with UNAM.== | |||
<StructureSection load='6eph' size='340' side='right'caption='[[6eph]], [[Resolution|resolution]] 2.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6eph]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EPH OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6EPH FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPZ:(2R)-2-{[(2R,3R,4R,5S,6R)-3-(ACETYLAMINO)-2-{[(S)-{[(R)-{[(2R,3S,4R,5R)-5-(2,4-DIOXO-3,4-DIHYDROPYRIMIDIN-1(2H)-YL)-3,4-DIHYDROXYTETRAHYDROFURAN-2-YL]METHOXY}(HYDROXY)PHOSPHORYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-5-HYDROXY-6-(HYDROXYMETHYL)TETRAHYDRO-2H-PYRAN-4-YL]OXY}PROPANOIC+ACID'>EPZ</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6eph FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6eph OCA], [http://pdbe.org/6eph PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6eph RCSB], [http://www.ebi.ac.uk/pdbsum/6eph PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6eph ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Bacterial toxin-antitoxin complexes are emerging as key players modulating bacterial physiology as activation of toxins induces stasis or programmed cell death by interference with vital cellular processes. Zeta toxins, which are prevalent in many bacterial genomes, were shown to interfere with cell wall formation by perturbing peptidoglycan synthesis in Gram-positive bacteria. Here, we characterize the epsilon/zeta toxin-antitoxin (TA) homologue from the Gram-negative pathogen Neisseria gonorrhoeae termed ng_varepsilon1 / ng_zeta1. Contrary to previously studied streptococcal epsilon/zeta TA systems, ng_varepsilon1 has an epsilon-unrelated fold and ng_zeta1 displays broader substrate specificity and phosphorylates multiple UDP-activated sugars that are precursors of peptidoglycan and lipopolysaccharide synthesis. Moreover, the phosphorylation site is different from the streptococcal zeta toxins, resulting in a different interference with cell wall synthesis. This difference most likely reflects adaptation to the individual cell wall composition of Gram-negative and Gram-positive organisms but also the distinct involvement of cell wall components in virulence. | |||
The ng_zeta1 toxin of the gonococcal epsilon/zeta toxin/antitoxin system drains precursors for cell wall synthesis.,Rocker A, Peschke M, Kittila T, Sakson R, Brieke C, Meinhart A Nat Commun. 2018 Apr 27;9(1):1686. doi: 10.1038/s41467-018-03652-8. PMID:29703974<ref>PMID:29703974</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6eph" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Meinhart, A]] | [[Category: Meinhart, A]] | ||
[[Category: Rocker, A]] | [[Category: Rocker, A]] | ||
[[Category: Bacterial toxin antitoxin system]] | |||
[[Category: Small molecule kinase]] | |||
[[Category: Toxin]] | |||
Latest revision as of 12:13, 11 November 2020
Structure of the epsilon_1 / zeta_1 antitoxin toxin system from Neisseria gonorrhoeae in complex with UNAM.Structure of the epsilon_1 / zeta_1 antitoxin toxin system from Neisseria gonorrhoeae in complex with UNAM.
Structural highlights
Publication Abstract from PubMedBacterial toxin-antitoxin complexes are emerging as key players modulating bacterial physiology as activation of toxins induces stasis or programmed cell death by interference with vital cellular processes. Zeta toxins, which are prevalent in many bacterial genomes, were shown to interfere with cell wall formation by perturbing peptidoglycan synthesis in Gram-positive bacteria. Here, we characterize the epsilon/zeta toxin-antitoxin (TA) homologue from the Gram-negative pathogen Neisseria gonorrhoeae termed ng_varepsilon1 / ng_zeta1. Contrary to previously studied streptococcal epsilon/zeta TA systems, ng_varepsilon1 has an epsilon-unrelated fold and ng_zeta1 displays broader substrate specificity and phosphorylates multiple UDP-activated sugars that are precursors of peptidoglycan and lipopolysaccharide synthesis. Moreover, the phosphorylation site is different from the streptococcal zeta toxins, resulting in a different interference with cell wall synthesis. This difference most likely reflects adaptation to the individual cell wall composition of Gram-negative and Gram-positive organisms but also the distinct involvement of cell wall components in virulence. The ng_zeta1 toxin of the gonococcal epsilon/zeta toxin/antitoxin system drains precursors for cell wall synthesis.,Rocker A, Peschke M, Kittila T, Sakson R, Brieke C, Meinhart A Nat Commun. 2018 Apr 27;9(1):1686. doi: 10.1038/s41467-018-03652-8. PMID:29703974[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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