7W1F
Crystal structure of the dNTP triphosphohydrolase PA1124 from Pseudomonas aeruginosa
Summary for 7W1F
| Entry DOI | 10.2210/pdb7w1f/pdb |
| Descriptor | Probable deoxyguanosinetriphosphate triphosphohydrolase, NICKEL (II) ION (2 entities in total) |
| Functional Keywords | dntp triphosphohydrolase, pa1124, pseudomonas aeruginosa, hydrolase |
| Biological source | Pseudomonas aeruginosa |
| Total number of polymer chains | 3 |
| Total formula weight | 172070.68 |
| Authors | Oh, H.B.,Song, W.S.,Lee, K.C.,Park, S.C.,Yoon, S.I. (deposition date: 2021-11-19, release date: 2022-03-23, Last modification date: 2023-11-29) |
| Primary citation | Oh, H.B.,Lee, K.C.,Park, S.C.,Song, W.S.,Yoon, S.I. Structural analysis of the dNTP triphosphohydrolase PA1124 from Pseudomonas aeruginosa. Biochem.Biophys.Res.Commun., 589:78-84, 2022 Cited by PubMed Abstract: dNTP triphosphohydrolase (TPH) belongs to the histidine/aspartate (HD) superfamily and catalyzes the hydrolysis of dNTPs into 2'-deoxyribonucleoside and inorganic triphosphate. TPHs are required for cellular dNTP homeostasis and DNA replication fidelity and are employed as a host defense mechanism. PA1124 from the pathogenic Pseudomonas aeruginosa bacterium functions as a dGTP and dTTP triphosphohydrolase. To reveal how PA1124 drives dNTP hydrolysis and is regulated, we performed a structural study of PA1124. PA1124 assembles into a hexameric architecture as a trimer of dimers. Each monomer has an interdomain dent where a metal ion is coordinated by conserved histidine and aspartate residues. A structure-based comparative analysis suggests that PA1124 accommodates the dNTP substrate into the interdomain dent near the metal ion. Interestingly, PA1124 interacts with ssDNA, presumably as an allosteric regulator, using a positively charged intersubunit cleft that is generated via dimerization. Furthermore, our phylogenetic analysis highlights similar or distinct oligomerization profiles across the TPH family. PubMed: 34894560DOI: 10.1016/j.bbrc.2021.12.002 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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