The role of short-range Cys171-Cys178 disulfide bond in maintaining cutinase active site integrity: a molecular dynamics simulation.
Understanding structural determinants in enzyme active site integrity can provide a good knowledge to design efficient novel catalytic machineries. Fusarium solani pisi cutinase with classic triad Ser-His-Asp is a promising enzyme to scrutinize these structural determinants. We performed two MD simulations: one, with the native structure, and the other with the broken Cys171-Cys178 disulfide bond. This disulfide bond stabilizes a turn in active site on which catalytic Asp175 is located. Functionally important H-bonds and atomic fluctuations in catalytic pocket have been changed. We proposed that this disulfide bond within active site can be considered as an important determinant of cutinase active site structural integrity.
Department of Biophysics, Faculty of Biological Science, Tarbiat Modares University, Tehran, Iran.
Mehdi Youssefi
MY
Matak
Majid Erfani
ME
Moghaddam
D002265:Carboxylic Ester Hydrolases / Q000737:chemistry*; D020134:Catalytic Domain; D003545:Cysteine / Q000737:chemistry*; D004220:Disulfides / Q000737:chemistry*; D004795:Enzyme Stability; D005670:Fusarium / Q000201:enzymology*; D006860:Hydrogen Bonding; D011487:Protein Conformation
D004220:Disulfides; D002265:Carboxylic Ester Hydrolases; C019952:cutinase; D003545:Cysteine