Modeling of the bacterial luciferase-flavin mononucleotide complex combining flexible docking with structure-activity data.

ABSTRACT: Although the crystal structure of Vibrio harveyi luciferase has been elucidated, the binding sites for the flavin mononucleotide and fatty aldehyde substrates are still unknown. The determined location of the phosphate-binding site close to Arg 107 on the alpha subunit of luciferase is supported here by point mutagenesis. This information, together with previous structure-activity data for the length of the linker connecting the phosphate group to the isoalloxazine ring represent important characteristics of the luciferase-bound conformation of the flavin mononucleotide. A model of the luciferase-flavin complex is developed here using flexible docking supplemented by these structural constraints. The location of the phosphate moiety was used as the anchor in a flexible docking procedure pe

SUBMITTER: Lin LY 

PROVIDER: S-EPMC2374094 | biostudies-literature | 2001 Aug

REPOSITORIES: biostudies-literature