1FY2

Aspartyl Dipeptidase

1FY2 の概要

• エントリーDOI: 10.2210/pdb1fy2/pdb
• 関連するPDBエントリー: 1FYE
• 分子名称: ASPARTYL DIPEPTIDASE, CADMIUM ION (3 entities in total)
• 機能のキーワード: serine protease, peptidase, catalytic triad, strand-helix motif, hydrolase
• 由来する生物種: Salmonella typhimurium
• 細胞内の位置: Cytoplasm: P36936
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24905.71

構造登録者

Hakansson, K.,Wang, A.H.-J.,Miller, C.G. (登録日: 2000-09-28, 公開日: 2001-01-10, 最終更新日: 2024-02-07)

主引用文献

Hakansson, K.,Wang, A.H.,Miller, C.G.
The structure of aspartyl dipeptidase reveals a unique fold with a Ser-His-Glu catalytic triad.
Proc.Natl.Acad.Sci.USA, 97:14097-14102, 2000

PubMed Abstract: The three-dimensional structure of Salmonella typhimurium aspartyl dipeptidase, peptidase E, was solved crystallographically and refined to 1.2-A resolution. The structure of this 25-kDa enzyme consists of two mixed beta-sheets forming a V, flanked by six alpha-helices. The active site contains a Ser-His-Glu catalytic triad and is the first example of a serine peptidase/protease with a glutamate in the catalytic triad. The active site Ser is located on a strand-helix motif reminiscent of that found in alpha/beta-hydrolases, but the polypeptide fold and the organization of the catalytic triad differ from those of the known serine proteases. This enzyme is a member of a family of serine hydrolases and appears to represent a new example of convergent evolution of peptidase activity.

PubMed: 11106384
DOI: 10.1073/pnas.260376797

実験手法

X-RAY DIFFRACTION (1.2 Å)