2B82

Crystal structure of AphA class B acid phosphatase/phosphotransferase ternary complex with adenosine and phosphate bound to the catalytic metal at 1.2 A resolution

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2B82 の概要

• エントリーDOI: 10.2210/pdb2b82/pdb
• 関連するPDBエントリー: 1N8N 1N9K 2B8J
• 分子名称: class B acid phosphatase, MAGNESIUM ION, PHOSPHATE ION, ... (5 entities in total)
• 機能のキーワード: class b acid phosphatase; dddd acid phosphatase; metallo-enzyme; amp, hydrolase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Periplasm (Potential): P32697
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 47709.56

構造登録者

Calderone, V.,Forleo, C.,Benvenuti, M.,Thaller, M.C.,Rossolini, G.M.,Mangani, S. (登録日: 2005-10-06, 公開日: 2005-11-29, 最終更新日: 2023-08-23)

主引用文献

Calderone, V.,Forleo, C.,Benvenuti, M.,Thaller, M.C.,Rossolini, G.M.,Mangani, S.
A structure-based proposal for the catalytic mechanism of the bacterial acid phosphatase AphA belonging to the DDDD superfamily of phosphohydrolases
J.Mol.Biol., 355:708-721, 2006

PubMed Abstract: The Escherichia coli gene aphA codes for a periplasmic acid phosphatase called AphA, belonging to class B bacterial phosphatases, which is part of the DDDD superfamily of phosphohydrolases. After our first report about its crystal structure, we have started a series of crystallographic studies aimed at understanding of the catalytic mechanism of the enzyme. Here, we report three crystal structures of the AphA enzyme in complex with the hydrolysis products of nucleoside monophosphate substrates and a fourth with a proposed intermediate analogue that appears to be covalently bound to the enzyme. Comparison with the native enzyme structure and with the available X-ray structures of different phosphatases provides clues about the enzyme chemistry and allows us to propose a catalytic mechanism for AphA, and to discuss it with respect to the mechanism of other bacterial and human phosphatases.

PubMed: 16330049
DOI: 10.1016/j.jmb.2005.10.068

実験手法

X-RAY DIFFRACTION (1.25 Å)