2FMJ

220-loop mutant of streptomyces griseus trypsin

2FMJ の概要

• エントリーDOI: 10.2210/pdb2fmj/pdb
• 関連するPDBエントリー: 1OS8 1OSS 1SGT
• 分子名称: Trypsin, CALCIUM ION, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: trypsin, serine protease, hydrolase
• 由来する生物種: Streptomyces griseus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23191.88

構造登録者

Page, M.J.,Di Cera, E. (登録日: 2006-01-09, 公開日: 2006-05-23, 最終更新日: 2024-10-30)

主引用文献

Page, M.J.,Bleackley, M.R.,Wong, S.,MacGillivray, R.T.,Di Cera, E.
Conversion of trypsin into a Na(+)-activated enzyme.
Biochemistry, 45:2987-2993, 2006

PubMed Abstract: Serine proteases of the chymotrypsin family show a dichotomous amino acid distribution for residue 225. Enzymes carrying Tyr at position 225 are activated by Na(+), whereas those carrying Pro are devoid of Na(+) binding and activation. Previous studies have demonstrated that the Y225P conversion is sufficient to abrogate Na(+) activation in several enzymes. However, the reverse substitution P225Y is necessary but not sufficient to introduce Na(+) binding and activation. Here we report that Streptomyces griseus trypsin, carrying Pro-225, can be engineered into a Na(+)-activated enzyme by replacing residues in the 170, 186, and 220 loops to those of coagulation factor Xa. The findings represent the first instance of an engineered Na(+)-activated enzyme and a proof of principle that should enable the design of other proteases with enhanced catalytic activity and allosteric regulation mediated by monovalent cation binding.

PubMed: 16503653
DOI: 10.1021/bi052481a

実験手法

X-RAY DIFFRACTION (1.65 Å)