1SKA

Crystallographic snapshots of Aspergillus fumigatus phytase revealing its enzymatic dynamics

1SKA の概要

• エントリーDOI: 10.2210/pdb1ska/pdb
• 関連するPDBエントリー: 1QWO 1SK8 1SK9 1SKB
• 分子名称: 3-phytase A, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• 機能のキーワード: small alpha domain, big alpha/beta domain, catalytic sites, water structures, catalytic dynamics, product release pathway, hydrolase
• 由来する生物種: Aspergillus fumigatus
• 細胞内の位置: Secreted: O00092
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 49208.11

構造登録者

Liu, Q.,Huang, Q.,Lei, X.G.,Hao, Q. (登録日: 2004-03-04, 公開日: 2004-09-28, 最終更新日: 2024-10-30)

主引用文献

Liu, Q.,Huang, Q.,Lei, X.G.,Hao, Q.
Crystallographic Snapshots of Aspergillus fumigatus Phytase, Revealing Its Enzymatic Dynamics
Structure, 12:1575-1583, 2004

PubMed Abstract: Understanding of the atomic movements involved in an enzymatic reaction needs structural information on the active and inactive native enzyme molecules and on the enzyme-substrate, enzyme-intermediate, and enzyme-product(s) complexes. By using the X-ray crystallographic method, four crystal structures of Aspergillus fumigatus phytase were obtained at resolution higher than 1.7 A. The pH-dependent catalytic activity of A. fumigatus phytase was linked to three water molecules that may prevent the substrate from binding and thus block nucleophilic attack of the catalytic imidazole nitrogen. Comparison of various structures also identified the water molecule that attacks the phosphamide bond during the hydrolysis process, and established the hydrolysis pathway of the intermediate. Additionally, two reaction product phosphates were observed at the active site, suggesting a possible product release pathway after hydrolysis of the intermediate. These results can help explain the catalytic mechanism throughout the whole acid phosphatase family, as all key residues are conserved.

PubMed: 15341723
DOI: 10.1016/j.str.2004.06.015

実験手法

X-RAY DIFFRACTION (1.69 Å)