Structure of Thermus thermophilus type 2 isopentenyl diphosphate isomerase inferred from crystallography and molecular dynamics

J. De Ruyck, S.C. Rothman, C.D. Poulter, J. Wouters

Research output: Contribution to journalArticle

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.
Original languageEnglish
Pages (from-to)1515-1518
Number of pages4
JournalBiochemical and Biophysical Research Communications
Volume338
Issue number3
DOIs
Publication statusPublished - 23 Dec 2005

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