Structure of Thermus thermophilus type 2 isopentenyl diphosphate isomerase inferred from crystallography and molecular dynamics.
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.
de Ruyck
Jérôme
J
Laboratoire de Chimie Biologique Structurale, University of Namur, B-5000 Namur, Belgium. jerome.deruyck@fundp.ac.be
Rothman
Steven C
SC
Poulter
C Dale
CD
Wouters
Johan
J
D019748:Carbon-Carbon Double Bond Isomerases / Q000737:chemistry* / Q000378:metabolism*; D002384:Catalysis; D018360:Crystallography, X-Ray; D045782:Hemiterpenes / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D009943:Organophosphorus Compounds / Q000737:chemistry / Q000378:metabolism; D020836:Protein Structure, Quaternary; D016963:Thermus thermophilus / Q000201:enzymology*
D045782:Hemiterpenes; D009943:Organophosphorus Compounds; C004809:isopentenyl pyrophosphate; D019748:Carbon-Carbon Double Bond Isomerases; C021453:isopentenyldiphosphate delta-isomerase