Structural highlights
Publication Abstract from PubMed
Tse2 is a cytoactive toxin secreted by a type six secretion apparatus of Pseudomonas aeruginosa. The Tse2 toxin naturally attacks a target in the cytoplasm of bacterial cells, and can cause toxicity if artificially introduced into eukaryotic cells. The X-ray crystal structure of the complex of Tse2 and its cognate immunity protein Tsi2 revealed a heterotetrameric structure with an extensive binding interface. Structural identity was found between Tse2 and NAD-dependent enzymes, especially ADP-ribosylating toxins, which facilitated the identification of the Tse2 active site and revealed it to be occluded upon binding the inhibitor Tsi2. The structural identity shared with NAD-dependent enzymes, including conserved catalytic residues, suggests that the mechanism of Tse2 toxicity may be NAD dependent.
The Structure of the Toxin and Type Six Secretion System Substrate Tse2 in Complex with Its Immunity Protein.,Robb CS, Robb M, Nano FE, Boraston AB Structure. 2015 Dec 28. pii: S0969-2126(15)00501-8. doi:, 10.1016/j.str.2015.11.012. PMID:26749446[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Robb CS, Robb M, Nano FE, Boraston AB. The Structure of the Toxin and Type Six Secretion System Substrate Tse2 in Complex with Its Immunity Protein. Structure. 2015 Dec 28. pii: S0969-2126(15)00501-8. doi:, 10.1016/j.str.2015.11.012. PMID:26749446 doi:http://dx.doi.org/10.1016/j.str.2015.11.012
