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.
|Number of pages||4|
|Journal||Biochemical and Biophysical Research Communications|
|Publication status||Published - 23 Dec 2005|
De Ruyck, J., Rothman, S. C., Poulter, C. D., & Wouters, J. (2005). Structure of Thermus thermophilus type 2 isopentenyl diphosphate isomerase inferred from crystallography and molecular dynamics. Biochemical and Biophysical Research Communications, 338(3), 1515-1518. https://doi.org/10.1016/j.bbrc.2005.10.114