Article ID Journal Published Year Pages File Type
10768876 Biochemical and Biophysical Research Communications 2005 4 Pages PDF
Abstract
Crystal structures of Thermus thermophilus and Bacillus subtilis type 2 IPP isomerases were combined to generate an almost complete model of the FMN-bound structure of the enzyme. In contrast to previous studies, positions of flexible loops were obtained and carefully analyzed by molecular dynamics. Docking simulations find a unique putative binding site for the IPP substrate.
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Life Sciences Biochemistry, Genetics and Molecular Biology Biochemistry
Preview
Structure of Thermus thermophilus type 2 isopentenyl diphosphate isomerase inferred from crystallography and molecular dynamics
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