3STQ
Hypothetical protein PA2703 Pseudomonas aeruginosa PAO1
Summary for 3STQ
| Entry DOI | 10.2210/pdb3stq/pdb |
| Descriptor | Putative uncharacterized protein (2 entities in total) |
| Functional Keywords | coiled-coil, toxin-antitoxin system, tsi2-tse2, t6ss, toxin immunity, toxin |
| Biological source | Pseudomonas aeruginosa |
| Total number of polymer chains | 6 |
| Total formula weight | 67886.78 |
| Authors | Zou, T.T.,Wang, M.T.,Jin, Q.,Cui, S. (deposition date: 2011-07-11, release date: 2012-02-08, Last modification date: 2024-03-20) |
| Primary citation | Zou, T.T.,Yao, X.,Qin, B.,Zhang, M.,Cai, L.F.,Shang, W.,Svergun, D.I.,Wang, M.T.,Cui, S.,Jin, Q. Crystal structure of Pseudomonas aeruginosa Tsi2 reveals a stably folded superhelical antitoxin J.Mol.Biol., 417:351-361, 2012 Cited by PubMed Abstract: In the competition for niches in natural resources, Pseudomonas aeruginosa utilizes the type VI secretion system to inject the toxic protein effector Tse2 into bacteria on cell-cell contact. The cytoplasm toxin immunity protein Tsi2 can neutralize Tse2 by physical interaction with the toxin, providing essential protection from toxin activity. Except for orthologues in P. aeruginosa, Tsi2 antitoxin does not share detectable sequence homology with known proteins in public databases. The mechanism underlying toxin neutralization by Tsi2 remains unknown. We report here the crystal structure of Tsi2 at 2.28 Å resolution. Our structural and biophysical analyses demonstrate that the antitoxin adopts a previously unobserved superhelical conformation. Tsi2 is highly thermostable in the absence of the toxin in solution. Tsi2 assembles a dimer with 2-fold rotational symmetry, similar to that observed in other toxin-antitoxin systems. Dimerization is essential for the stable folding of Tsi2. PubMed: 22310046DOI: 10.1016/j.jmb.2012.01.040 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.284 Å) |
Structure validation
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