1DKP

CRYSTAL STRUCTURE OF PHYTATE COMPLEX OF ESCHERICHIA COLI PHYTASE AT PH 6.6. PHYTATE IS BOUND WITH ITS 3-PHOSPHATE IN THE ACTIVE SITE. HG2+ CATION ACTS AS AN INTERMOLECULAR BRIDGE

1DKP の概要

• エントリーDOI: 10.2210/pdb1dkp/pdb
• 関連するPDBエントリー: 1DKL 1DKM 1DKN 1DKO 1DKQ
• 分子名称: PHYTASE, MERCURY (II) ION, INOSITOL HEXAKISPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: histidine acid phosphatase fold, hydrolase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 46159.00

構造登録者

Lim, D.,Golovan, S.,Forsberg, C.W.,Jia, Z. (登録日: 1999-12-08, 公開日: 2000-08-03, 最終更新日: 2024-10-30)

主引用文献

Lim, D.,Golovan, S.,Forsberg, C.W.,Jia, Z.
Crystal structures of Escherichia coli phytase and its complex with phytate.
Nat.Struct.Biol., 7:108-113, 2000

PubMed Abstract: Phytases catalyze the hydrolysis of phytate and are able to improve the nutritional quality of phytate-rich diets. Escherichia coli phytase, a member of the histidine acid phosphatase family has the highest specific activity of all phytases characterized. The crystal structure of E. coli phytase has been determined by a two-wavelength anomalous diffraction method using the exceptionally strong anomalous scattering of tungsten. Despite a lack of sequence similarity, the structure closely resembles the overall fold of other histidine acid phosphatases. The structure of E. coli phytase in complex with phytate, the preferred substrate, reveals the binding mode and substrate recognition. The binding is also accompanied by conformational changes which suggest that substrate binding enhances catalysis by increasing the acidity of the general acid.

PubMed: 10655611
DOI: 10.1038/72371

実験手法

X-RAY DIFFRACTION (2.28 Å)