2FHM

Solution Structure of Bacillus subtilis Acylphosphatase

2FHM の概要

• エントリーDOI: 10.2210/pdb2fhm/pdb
• NMR情報: BMRB: 6884
• 分子名称: Probable acylphosphatase (1 entity in total)
• 機能のキーワード: acylphosphatase, hydrolase
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10332.69

構造登録者

Xia, B.,Hu, J.C. (登録日: 2005-12-26, 公開日: 2007-01-02, 最終更新日: 2024-05-01)

主引用文献

Hu, J.C.,Li, D.,Su, X.-D.,Jin, C.W.,Xia, B.
Solution structure and conformational heterogeneity of acylphosphatase from Bacillus subtilis
Febs Lett., 584:2852-2856, 2010

PubMed Abstract: Acylphosphatase is a small enzyme that catalyzes the hydrolysis of acyl phosphates. Here, we present the solution structure of acylphosphatase from Bacillus subtilis (BsAcP), the first from a Gram-positive bacterium. We found that its active site is disordered, whereas it converted to an ordered state upon ligand binding. The structure of BsAcP is sensitive to pH and it has multiple conformations in equilibrium at acidic pH (pH<5.8). Only one main conformation could bind ligand, and the relative population of these states is modulated by ligand concentration. This study provides direct evidence for the role of ligand in conformational selection.

PubMed: 20447399
DOI: 10.1016/j.febslet.2010.04.069

実験手法

SOLUTION NMR