8JGO

Crystal structure of Deinococcus radiodurans exopolyphosphatase

8JGO の概要

• エントリーDOI: 10.2210/pdb8jgo/pdb
• 分子名称: Exopolyphosphatase, SULFATE ION, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: polyphosphate, exopolyphosphatase, hydrolase
• 由来する生物種: Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 57335.71

構造登録者

Zhao, Y.,Dai, S. (登録日: 2023-05-21, 公開日: 2024-05-15, 最終更新日: 2024-07-31)

主引用文献

Dai, S.,Wang, B.,Ye, R.,Zhang, D.,Xie, Z.,Yu, N.,Cai, C.,Huang, C.,Zhao, J.,Zhang, F.,Hua, Y.,Zhao, Y.,Zhou, R.,Tian, B.
Structural Evolution of Bacterial Polyphosphate Degradation Enzyme for Phosphorus Cycling.
Adv Sci, 11:e2309602-e2309602, 2024

PubMed Abstract: Living organisms ranging from bacteria to animals have developed their own ways to accumulate and store phosphate during evolution, in particular as the polyphosphate (polyP) granules in bacteria. Degradation of polyP into phosphate is involved in phosphorus cycling, and exopolyphosphatase (PPX) is the key enzyme for polyP degradation in bacteria. Thus, understanding the structure basis of PPX is crucial to reveal the polyP degradation mechanism. Here, it is found that PPX structure varies in the length of ɑ-helical interdomain linker (ɑ-linker) across various bacteria, which is negatively correlated with their enzymatic activity and thermostability - those with shorter ɑ-linkers demonstrate higher polyP degradation ability. Moreover, the artificial DrPPX mutants with shorter ɑ-linker tend to have more compact pockets for polyP binding and stronger subunit interactions, as well as higher enzymatic efficiency (k/K) than that of DrPPX wild type. In Deinococcus-Thermus, the PPXs from thermophilic species possess a shorter ɑ-linker and retain their catalytic ability at high temperatures (70 °C), which may facilitate the thermophilic species to utilize polyP in high-temperature environments. These findings provide insights into the interdomain linker length-dependent evolution of PPXs, which shed light on enzymatic adaption for phosphorus cycling during natural evolution and rational design of enzyme.

PubMed: 38682481
DOI: 10.1002/advs.202309602

実験手法

X-RAY DIFFRACTION (1.9 Å)