9G8T
Crystal structure of the persulfide dioxygenase (PDO - PA2915) from Pseudomonas aeruginosa
Summary for 9G8T
| Entry DOI | 10.2210/pdb9g8t/pdb |
| Descriptor | Metallo-beta-lactamase domain-containing protein, DI(HYDROXYETHYL)ETHER, ZINC ION, ... (5 entities in total) |
| Functional Keywords | persulfide, gsh, gssh, nitric oxide, beta-lactamase mbl, oxidoreductase |
| Biological source | Pseudomonas aeruginosa |
| Total number of polymer chains | 1 |
| Total formula weight | 33366.85 |
| Authors | Troilo, F.,Giordano, F.,Giuffre, A.,Giardina, G.,Di Matteo, A. (deposition date: 2024-07-24, release date: 2025-08-06, Last modification date: 2026-02-18) |
| Primary citation | Giordano, F.,Troilo, F.,Nastasi, M.R.,Caruso, L.,Mellini, M.,Travaglini-Allocatelli, C.,Giardina, G.,Vicente, J.B.,Rampioni, G.,Di Matteo, A.,Forte, E.,Giuffre, A. Structure and function of persulfide dioxygenase from Pseudomonas aeruginosa : Implications on H 2 S homeostasis and interplay with nitric oxide. Iscience, 29:114586-114586, 2026 Cited by PubMed Abstract: Hydrogen sulfide is an important signaling molecule, beneficial at physiological concentrations but harmful at higher levels, due to which a tight control of its bioavailability is essential. Here, we investigated persulfide dioxygenase, an enzyme involved in HS catabolism, from the pathogen (PDO). Deletion of the gene led to a 4-fold increase in HS concentration, confirming its physiological role. The recombinant enzyme was structurally characterized at 2.06 Å resolution and assigned to the metallo-β-lactamase superfamily. Compared with its human homolog, PDO displayed a different dimerization area and a larger active site, suggesting different substrate preferences. Functionally, PDO catalyzed glutathione persulfide dioxygenation with a high turnover rate, and its activity was enhanced by reduced glutathione. Interestingly, the results show that PDO binds to nitric oxide, which reversibly inhibits its catalytic activity. These findings reveal a novel mechanism of crosstalk between hydrogen sulfide and nitric oxide signaling and provide insights into redox regulation in a multidrug-resistant pathogen. PubMed: 41623452DOI: 10.1016/j.isci.2025.114586 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.06 Å) |
Structure validation
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