2FHM

Solution Structure of Bacillus subtilis Acylphosphatase

Summary for 2FHM

• Entry DOI: 10.2210/pdb2fhm/pdb
• NMR Information: BMRB: 6884
• Descriptor: Probable acylphosphatase (1 entity in total)
• Functional Keywords: acylphosphatase, hydrolase
• Biological source: Bacillus subtilis
• Total number of polymer chains: 1
• Total formula weight: 10332.69

Authors

Xia, B.,Hu, J.C. (deposition date: 2005-12-26, release date: 2007-01-02, Last modification date: 2024-05-01)

Primary citation

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

Experimental method

SOLUTION NMR