1N9K

Crystal structure of the bromide adduct of AphA class B acid phosphatase/phosphotransferase from E. coli at 2.2 A resolution

1N9K の概要

• エントリーDOI: 10.2210/pdb1n9k/pdb
• 関連するPDBエントリー: 1N8N
• 分子名称: Class B acid phosphatase, MAGNESIUM ION, BROMIDE ION, ... (4 entities in total)
• 機能のキーワード: class b acid phosphatase, dddd acid phosphatase, metallo-enzyme bromide mad, hydrolase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 48357.85

構造登録者

Calderone, V.,Forleo, C.,Benvenuti, M.,Rossolini, G.M.,Thaller, M.C.,Mangani, S. (登録日: 2002-11-25, 公開日: 2004-02-03, 最終更新日: 2024-02-14)

主引用文献

Calderone, V.,Forleo, C.,Benvenuti, M.,Thaller, M.C.,Rossolini, G.M.,Mangani, S.
The first structure of a bacterial class B Acid phosphatase reveals further structural heterogeneity among phosphatases of the haloacid dehalogenase fold.
J.Mol.Biol., 335:761-773, 2004

PubMed Abstract: AphA is a periplasmic acid phosphatase of Escherichia coli belonging to class B bacterial phosphatases, which is part of the DDDD superfamily of phosphohydrolases. The crystal structure of AphA has been determined at 2.2A and its resolution extended to 1.7A on an AuCl(3) derivative. This represents the first crystal structure of a class B bacterial phosphatase. Despite the lack of sequence homology, the AphA structure reveals a haloacid dehalogenase-like fold. This finding suggests that this fold could be conserved among members of the DDDD superfamily of phosphohydrolases. The active enzyme is a homotetramer built by using an extended N-terminal arm intertwining the four monomers. The active site of the native enzyme, as prepared, hosts a magnesium ion, which can be replaced by other metal ions. The structure explains the non-specific behaviour of AphA towards substrates, while a structure-based alignment with other phosphatases provides clues about the catalytic mechanism.

PubMed: 14687572
DOI: 10.1016/j.jmb.2003.10.050

実験手法

X-RAY DIFFRACTION (2.2 Å)