6AG4

Crystal structure of Ard1 N-terminal acetyltransferase H88A/E127A mutant from Sulfolobus solfataricus

6AG4 の概要

• エントリーDOI: 10.2210/pdb6ag4/pdb
• 分子名称: N-alpha-acetyltransferase, ACETYL COENZYME *A, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: acetyltransferase, transferase
• 由来する生物種: Sulfolobus solfataricus P2
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21123.05

構造登録者

Chang, Y.Y.,Hsu, C.H. (登録日: 2018-08-09, 公開日: 2019-08-14, 最終更新日: 2023-11-22)

主引用文献

Chang, Y.Y.,Hagawa, S.,Hsu, C.H.
Adaptation of thermophilic acetyltransferase to a water-mediated catalytic mechanism.
Chem.Commun.(Camb.), 56:10537-10540, 2020

PubMed Abstract: The common mechanism of N-acetyltransferases (NATs) is a water-mediated catalysis, which is not conducive to thermophilic acetyltransferases. The crystal structure of SsArd1 shows an ordered catalytic water molecule in a trap formed by the residues H88 and E127. Structure-guided mutagenesis, kinetic studies and MD simulation indicated that the turnover rates of H88A, E127A and H88A/E127A mutants were low, but that of the H88E/E127H mutant could be restored to the level of the wild type.

PubMed: 32780067
DOI: 10.1039/d0cc04305b

実験手法

X-RAY DIFFRACTION (2.256 Å)