4X8I

de novo crystal structure of the Pyrococcus Furiosus TET3 aminopeptidase

4X8I の概要

• エントリーDOI: 10.2210/pdb4x8i/pdb
• 分子名称: Lysyl aminopeptidase, ZINC ION, COBALT (II) ION, ... (7 entities in total)
• 機能のキーワード: aminopeptidase, hydrolase
• 由来する生物種: Pyrococcus furiosus
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 117405.72

構造登録者

Colombo, M. (登録日: 2014-12-10, 公開日: 2016-02-10, 最終更新日: 2024-05-08)

主引用文献

Colombo, M.,Girard, E.,Franzetti, B.
Tuned by metals: the TET peptidase activity is controlled by 3 metal binding sites.
Sci Rep, 6:20876-20876, 2016

PubMed Abstract: TET aminopeptidases are dodecameric particles shared in the three life domains involved in various biological processes, from carbon source provider in archaea to eye-pressure regulation in humans. Each subunit contains a dinuclear metal site (M1 and M2) responsible for the enzyme catalytic activity. However, the role of each metal ion is still uncharacterized. Noteworthy, while mesophilic TETs are activated by Mn(2+), hyperthermophilic TETs prefers Co(2+). Here, by means of anomalous x-ray crystallography and enzyme kinetics measurements of the TET3 aminopeptidase from the hyperthermophilic organism Pyrococcus furiosus (PfTET3), we show that M2 hosts the catalytic activity of the enzyme, while M1 stabilizes the TET3 quaternary structure and controls the active site flexibility in a temperature dependent manner. A new third metal site (M3) was found in the substrate binding pocket, modulating the PfTET3 substrate preferences. These data show that TET activity is tuned by the molecular interplay among three metal sites.

PubMed: 26853450
DOI: 10.1038/srep20876

実験手法

X-RAY DIFFRACTION (2.5 Å)