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....

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Veröffentlicht in:	Biochemical and biophysical research communications 2005-12, Vol.338 (3), p.1515-1518
Hauptverfasser:	de Ruyck, Jérôme, Rothman, Steven C., Poulter, C. Dale, Wouters, Johan
Format:	Artikel
Sprache:	eng
Schlagworte:	Bacillus subtilis Carbon-Carbon Double Bond Isomerases - chemistry Carbon-Carbon Double Bond Isomerases - metabolism Catalysis Crystallography, X-Ray Flavoprotein Hemiterpenes - chemistry Hemiterpenes - metabolism IDI-2 Macromolecules crystallography Models, Molecular Molecular modelling Organophosphorus Compounds - chemistry Organophosphorus Compounds - metabolism Protein Structure, Quaternary Thermus thermophilus Thermus thermophilus - enzymology
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Beschreibung
Zusammenfassung:	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.
ISSN:	0006-291X 1090-2104
DOI:	10.1016/j.bbrc.2005.10.114