Pressure Affects the Structure and the Dynamics of the D-Galactose/D-Glucose-Binding Protein from Escherichia coli by Perturbing the C-Terminal Dom
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- 作者：Anna Marabotti ; Alessio Ausili ; Maria Staiano ; Andrea Scirè ; Fabio Tanfani ; Antonietta Parracino ; Antonio Varriale ; Mosè ; Rossi ; Sabato D'Auria
- 刊名：Biochemistry
- 出版年：2006
- 出版时间：October 3, 2006
- 年：2006
- 卷：45
- 期：39
- 页码：11885 - 11894
- 全文大小：707K
- 年卷期：v.45,no.39(October 3, 2006)
- ISSN：1520-4995
文摘
The effect of the pressure on the structure and stability of the D-galactose/D-glucose bindingprotein from Escherichia coli in the absence (GGBP) and in the presence (GGBP/Glc) of glucose wasstudied by Fourier transform infrared (FT-IR) spectroscopy and molecular dynamic (MD) simulations.FT-IR spectroscopy experiments showed that the protein 
-structures are more resistant than 
-helicesstructures to pressure value increases. In addition, the infrared data indicated that the binding of glucosestabilizes the protein structure against high pressure values, and the protein structure does not completelyunfold up to pressure values close to 9000 bar. MD simulations allow a prediction of the most probableconfiguration of the protein, consistent with the increasing pressures on the two systems. The detailedanalysis of the structures at molecular level confirms that, among secondary structures, -helices aremore sensitive than -structures to the destabilizing effect of high pressure and that glucose is able topreserve the structure of the protein in the complex. Moreover, the evidence of the different resistance ofthe two domains of this protein to high pressure is investigated and explained at a molecular level, indicatingthe importance of aromatic amino acid in protein stabilization.
-structures are more resistant than -helicesstructures to pressure value increases. In addition, the infrared data indicated that the binding of glucosestabilizes the protein structure against high pressure values, and the protein structure does not completelyunfold up to pressure values close to 9000 bar. MD simulations allow a prediction of the most probableconfiguration of the protein, consistent with the increasing pressures on the two systems. The detailedanalysis of the structures at molecular level confirms that, among secondary structures, -helices aremore sensitive than -structures to the destabilizing effect of high pressure and that glucose is able topreserve the structure of the protein in the complex. Moreover, the evidence of the different resistance ofthe two domains of this protein to high pressure is investigated and explained at a molecular level, indicatingthe importance of aromatic amino acid in protein stabilization.