Model of the active site of firefly luciferase.
A model for the spatial structure of firefly luciferase--ATP--luciferin complex is suggested using the coordinates of unliganded luciferase and the enzyme--substrate complex of the adenylating subunit of gramicidin S synthetase known from the literature. Conformational changes in luciferase can occur during substrate binding resulting in a relative orientation of two luciferase domains similar to that in case of the AMP--phenylalanine--synthetase complex. The model is consistent with data on the physicochemical properties of firefly luciferase and its complexes with the substrates.
Sandalova
T P
TP
Institute of Biophysics, Siberian Branch of the Russian Academy of Sciences, Krasnoyarsk, 660036, Russia.
Ugarova
N N
NN
D000255:Adenosine Triphosphate / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D001517:Coleoptera / Q000201:enzymology; D049454:Firefly Luciferin / Q000378:metabolism; D008156:Luciferases / Q000737:chemistry* / Q000378:metabolism; D046911:Macromolecular Substances; D008958:Models, Molecular; D011487:Protein Conformation
D046911:Macromolecular Substances; D049454:Firefly Luciferin; D000255:Adenosine Triphosphate; D008156:Luciferases