6EPI
Structure of the epsilon_1 / zeta_1 antitoxin / toxin system from Neisseria gonorrhoeae in complex with UNAM-4P.
Summary for 6EPI
| Entry DOI | 10.2210/pdb6epi/pdb |
| Descriptor | Epsilon_1 antitoxin, Zeta_1 toxin, UDP-N-acetyl-muramic acid-4'phosphate, ... (6 entities in total) |
| Functional Keywords | bacterial toxin antitoxin systems, small molecule kinases, toxin |
| Biological source | Neisseria gonorrhoeae More |
| Total number of polymer chains | 8 |
| Total formula weight | 212275.08 |
| Authors | Rocker, A.,Meinhart, A. (deposition date: 2017-10-11, release date: 2018-05-02, Last modification date: 2024-01-17) |
| Primary citation | Rocker, A.,Peschke, M.,Kittila, T.,Sakson, R.,Brieke, C.,Meinhart, A. The ng_ zeta 1 toxin of the gonococcal epsilon/zeta toxin/antitoxin system drains precursors for cell wall synthesis. Nat Commun, 9:1686-1686, 2018 Cited by PubMed Abstract: 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_ɛ1 / ng_ζ1. Contrary to previously studied streptococcal epsilon/zeta TA systems, ng_ɛ1 has an epsilon-unrelated fold and ng_ζ1 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. PubMed: 29703974DOI: 10.1038/s41467-018-03652-8 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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