7KYD

Drosophila melanogaster long-chain fatty-acyl-CoA synthetase CG6178

Summary for 7KYD

• Entry DOI: 10.2210/pdb7kyd/pdb
• Descriptor: Long-chain fatty-acyl-CoA synthetase CG6178, 5'-O-[(S)-hydroxy(octanoyloxy)phosphoryl]adenosine, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: luciferase, hydrolase, ligase
• Biological source: Drosophila melanogaster (fruit fly)
• Total number of polymer chains: 1
• Total formula weight: 60957.48

Authors

Adams, S.T.,Zephyr, J.,Bohn, M.F.,Schiffer, C.A.,Miller, S.C. (deposition date: 2020-12-07, release date: 2022-01-05, Last modification date: 2023-10-25)

Primary citation

Adams, S.T.,Zephyr, J.,Bohn, M.F.,Schiffer, C.A.,Miller, S.C.
FruitFire: a luciferase based on a fruit fly metabolic enzyme.
Biorxiv, 2023

PubMed Abstract: Firefly luciferase is homologous to fatty acyl-CoA synthetases from insects that are not bioluminescent. Here, we determined the crystal structure of the fruit fly fatty acyl-CoA synthetase CG6178 to 2.5 Å. Based on this structure, we mutated a steric protrusion in the active site to create the artificial luciferase FruitFire, which prefers the synthetic luciferin CycLuc2 to d-luciferin by >1000-fold. FruitFire enabled in vivo bioluminescence imaging in the brains of mice using the pro-luciferin CycLuc2-amide. The conversion of a fruit fly enzyme into a luciferase capable of in vivo imaging underscores the potential for bioluminescence with a range of adenylating enzymes from nonluminescent organisms, and the possibilities for application-focused design of enzyme-substrate pairs.

PubMed: 37425765
DOI: 10.1101/2023.06.30.547126

Experimental method

X-RAY DIFFRACTION (2.5 Å)