Sandbox Reserved 1731

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This Sandbox is Reserved from August 30, 2022 through May 31, 2023 for use in the course Biochemistry I taught by Kimberly Lane at the Radford University, Radford, VA, USA. This reservation includes Sandbox Reserved 1730 through Sandbox Reserved 1749.

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Contents 1 Photinus pyralis luciferase 2 Structure 3 Function 4 Biological Application 5 Structural highlights 6 References

Photinus pyralis luciferase

spinqualitylabelsall models Structure of Photinus pyralis luciferase (PDB entry 1LCI) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Luciferases are enzymes that catalyzes the light-producing chemical reactions of bioluminescent organisms, such as fireflies and bacteria. Photinus pyralis luciferase, which is the specific luciferase protein found in the common eastern firefly, causes an enzymatic reaction between the enzyme (luciferase) and the substrate (luciferin). This reaction is an oxidation process with molecular oxygen and its conversion into chemical energy, which causes the bursts of light.

Structure

The overall structure of luciferase is an asymmetrical monomer. It is composed of two domains specified as the N-terminal and C-terminal. The N-terminal domain consists of a beta-barrel and two beta-sheets flanked by alpha-helices to form a five layer structure α-β-α-β-α structure. The C-terminal domain consists of five beta-strands and three alpha-helices, which is folded into a compact structure that is connected to the N-terminus domain by a disordered loop. Luciferase is composed of 550 amino acids residues in a single polypeptide chain with a peroxisome targeting signal sequence of -Ser-Lys-Leu (-SKL) at C-terminus. The overall structure of luciferase contains alpha helices and beta-barrels.

Function

Biological Application

Structural highlights

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References