9R0Q
Paraoxonase-1 in complex with terbium(III) and 2-hydroxyquinoline
Summary for 9R0Q
| Entry DOI | 10.2210/pdb9r0q/pdb |
| Descriptor | Serum paraoxonase/arylesterase 1, TERBIUM(III) ION, CALCIUM ION, ... (6 entities in total) |
| Functional Keywords | hydrolase, enzyme:inhibitor complex |
| Biological source | Oryctolagus cuniculus (rabbit) |
| Total number of polymer chains | 1 |
| Total formula weight | 40997.60 |
| Authors | Smerkolj, J.,Pavsic, M.,Golicnik, M. (deposition date: 2025-04-24, release date: 2025-08-06, Last modification date: 2025-08-27) |
| Primary citation | Smerkolj, J.,Bahun, M.,Poklar Ulrih, N.,Bavec, A.,Pavsic, M.,Golicnik, M. Intramolecular sensitization and structure of a Tb 3+ /2-hydroxyquinoline conjugate in the paraoxonase 1 active site. Dalton Trans, 54:12471-12481, 2025 Cited by PubMed Abstract: Paraoxonase 1 (PON1) is a Ca-dependent enzyme involved in oxidative stress processes and is widely studied for its protective roles in various diseases. Intermolecular sensitization of lanthanide ions was implemented by replacing Ca ions from the recombinant PON1 (rePON1) catalytic site in the presence of 2-hydroxyquinoline (2HQ) as an external antenna. Although the replacement of Ca ions with lanthanide ions indicates weaker binding affinity for the coordination of 2HQ in the protein milieu of the rePON1 active site, it results in the formation of a highly emissive supramolecular complex in the case of Tb ions. The architecture of the ternary rePON1 : Tb : 2HQ conjugate, which allows efficient terbium sensitization and its specific long-wavelength metal phosphorescence emission, was resolved by X-ray crystallography. These findings could establish a non-catalytic quantification strategy for PON1 and provide additional structural insights into lanthanide substitution in this Ca-dependent enzyme. PubMed: 40735812DOI: 10.1039/d5dt01484k PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.35 Å) |
Structure validation
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