2DEA

Crystal Structure of the Aminopeptidase of Aeromonas proteolytica at pH 4.7

2DEA の概要

• エントリーDOI: 10.2210/pdb2dea/pdb
• 関連するPDBエントリー: 1FT7 1LOK 1RTQ 1TXR
• 分子名称: Bacterial leucyl aminopeptidase, ZINC ION, SODIUM ION, ... (4 entities in total)
• 機能のキーワード: aminopeptidase, metalloenzyme, bimetalloenzyme, low ph, zinc enzyme, hydrolase
• 由来する生物種: Vibrio proteolyticus
• 細胞内の位置: Secreted: Q01693
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 32391.96

構造登録者

Petsko, G.A.,Ringe, D.,Desmarais, W. (登録日: 2006-02-10, 公開日: 2006-07-25, 最終更新日: 2024-10-30)

主引用文献

Desmarais, W.,Bienvenue, D.L.,Bzymek, K.P.,Petsko, G.A.,Ringe, D.,Holz, R.C.
The high-resolution structures of the neutral and the low pH crystals of aminopeptidase from Aeromonas proteolytica.
J.Biol.Inorg.Chem., 11:398-408, 2006

PubMed Abstract: The aminopeptidase from Aeromonas proteolytica (AAP) contains two zinc ions in the active site and catalyzes the degradation of peptides. Herein we report the crystal structures of AAP at 0.95-A resolution at neutral pH and at 1.24-A resolution at low pH. The combination of these structures allowed the precise modeling of atomic positions, the identification of the metal bridging oxygen species, and insight into the physical properties of the metal ions. On the basis of these structures, a new putative catalytic mechanism is proposed for AAP that is likely relevant to all binuclear metalloproteases.

PubMed: 16596389
DOI: 10.1007/s00775-006-0093-x

実験手法

X-RAY DIFFRACTION (1.24 Å)