3CZ4

Native AphA class B acid phosphatase/phosphotransferase from E. coli

3CZ4 の概要

• エントリーDOI: 10.2210/pdb3cz4/pdb
• 関連するPDBエントリー: 1n8n 1n9k 1rmq 1rmy 2g1a 2hf7
• 分子名称: Class B acid phosphatase, MAGNESIUM ION, ACETATE ION, ... (6 entities in total)
• 機能のキーワード: hydrolase, acid phosphatase/phosphotransferase, metallo phosphatase, magnesium, metal-binding, periplasm
• 由来する生物種: Escherichia coli
• 細胞内の位置: Periplasm (Potential): P0AE22
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24008.79

構造登録者

Leone, R.,Cappelletti, E.,Benvenuti, M.,Lentini, G.,Thaller, M.C.,Mangani, S. (登録日: 2008-04-28, 公開日: 2008-11-11, 最終更新日: 2023-08-30)

主引用文献

Leone, R.,Cappelletti, E.,Benvenuti, M.,Lentini, G.,Thaller, M.C.,Mangani, S.
Structural insights into the catalytic mechanism of the bacterial class B phosphatase AphA belonging to the DDDD superfamily of phosphohydrolases.
J.Mol.Biol., 384:478-488, 2008

PubMed Abstract: AphA is a magnesium-dependent, bacterial class B acid phosphatase that catalyzes the hydrolysis of a variety of phosphoester substrates and belongs to the DDDD superfamily of phosphohydrolases. The recently reported crystal structure of AphA from Escherichia coli has revealed the quaternary structure of the enzyme together with hints about its catalytic mechanism. The present work reports the crystal structures of AphA from E. coli in complex with substrate, transition-state, and intermediate analogues. The structures provide new insights into the mechanism of the enzyme and allow a revision of some aspects of the previously proposed mechanism that have broader implications for all the phosphatases of the DDDD superfamily.

PubMed: 18845157
DOI: 10.1016/j.jmb.2008.09.050

実験手法

X-RAY DIFFRACTION (1.7 Å)