Three-dimensional model of the alpha-subunit of bacterial luciferase.
The predicted secondary structure of both subunits of bacterial luciferase is in accordance with a regular 8-fold alpha/beta-barrel structure. The 3D profile confirmed that luciferase subunits are compatible with the alpha/beta-barrel despite the absence of sequence similarity with any alpha/beta-barrel protein. The three-dimensional structure of 260 residues of the alpha-chain of luciferase was modeled from coordinates of glycolate oxidase and then energy minimized. The model obtained satisfies the criteria for the structure of a globular protein and is in accordance with known experimental data. From the model it is possible to predict active site residues involved in binding and catalysis. These predictions, and thus also the model, can be tested by protein engineering experiments.
Sandalova
T
T
Department of Molecular Biology, Swedish University of Agricultural Sciences, Uppsala, Sweden.
Lindqvist
Y
Y
D000447:Aldehydes / Q000378:metabolism; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D005486:Flavin Mononucleotide / Q000378:metabolism; D005415:Flavins / Q000378:metabolism; D005949:Glucose Oxidase / Q000737:chemistry; D008156:Luciferases / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010710:Phosphates / Q000378:metabolism; D010776:Photobacterium / Q000201:enzymology*; D011485:Protein Binding; D017433:Protein Structure, Secondary; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013698:Templates, Genetic
D000447:Aldehydes; D001426:Bacterial Proteins; D005415:Flavins; D010710:Phosphates; C008173:isoalloxazine; D005486:Flavin Mononucleotide; D005949:Glucose Oxidase; D008156:Luciferases