Structure of bacterial luciferase.
The generation of light by living organisms such as fireflies, glow-worms, mushrooms, fish, or bacteria growing on decaying materials has been a subject of fascination throughout the ages, partly because it occurs without the need for high temperatures. The chemistry behind the numerous bioluminescent systems is quite varied, and the enzymes that catalyze the reactions, the luciferases, are a large and evolutionarily diverse group. The structure of the best understood of these intriguing enzymes, bacterial luciferase, has recently been determined, allowing discussion of features of the protein in structural terms for the first time.
Baldwin
T O
TO
Texas A&M University, College Station, USA.
Christopher
J A
JA
Raushel
F M
FM
Sinclair
J F
JF
Ziegler
M M
MM
Fisher
A J
AJ
Rayment
I
I
D001419:Bacteria / Q000201:enzymology*; D001665:Binding Sites; D005486:Flavin Mononucleotide / Q000378:metabolism; D006860:Hydrogen Bonding; D007700:Kinetics; D008156:Luciferases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D008163:Luminescent Measurements; D008958:Models, Molecular; D010100:Oxygen / Q000378:metabolism; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary
D005486:Flavin Mononucleotide; D008156:Luciferases; D010100:Oxygen