7W1F

Crystal structure of the dNTP triphosphohydrolase PA1124 from Pseudomonas aeruginosa

7W1F の概要

• エントリーDOI: 10.2210/pdb7w1f/pdb
• 分子名称: Probable deoxyguanosinetriphosphate triphosphohydrolase, NICKEL (II) ION (2 entities in total)
• 機能のキーワード: dntp triphosphohydrolase, pa1124, pseudomonas aeruginosa, hydrolase
• 由来する生物種: Pseudomonas aeruginosa
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 172070.68

構造登録者

Oh, H.B.,Song, W.S.,Lee, K.C.,Park, S.C.,Yoon, S.I. (登録日: 2021-11-19, 公開日: 2022-03-23, 最終更新日: 2023-11-29)

主引用文献

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

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: 34894560
DOI: 10.1016/j.bbrc.2021.12.002

実験手法

X-RAY DIFFRACTION (2.9 Å)