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6K4D

Ancestral luciferase AncLamp in complex with ATP and D-luciferin

Summary for 6K4D
Entry DOI10.2210/pdb6k4d/pdb
DescriptorAncestral luciferase AncLamp, [[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] (4S)-2-(6-oxidanyl-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylate, (4S)-2-(6-hydroxy-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-4-carboxylic acid, ... (4 entities in total)
Functional Keywordsluciferase, bioluminescence, ancestral protein, molecular evolution, oxidoreductase
Biological sourceLampyridae
Total number of polymer chains1
Total formula weight61264.22
Authors
Oba, Y.,Konishi, K.,Yano, D.,Kato, D.,Shirai, T. (deposition date: 2019-05-23, release date: 2020-05-27, Last modification date: 2023-11-22)
Primary citationOba, Y.,Konishi, K.,Yano, D.,Shibata, H.,Kato, D.,Shirai, T.
Resurrecting the ancient glow of the fireflies.
Sci Adv, 6:-, 2020
Cited by
PubMed Abstract: The color of firefly bioluminescence is determined by the structure of luciferase. Firefly luciferase genes have been isolated from more than 30 species, producing light ranging in color from green to orange-yellow. Here, we reconstructed seven ancestral firefly luciferase genes, characterized the enzymatic properties of the recombinant proteins, and determined the crystal structures of the gene from ancestral Lampyridae. Results showed that the synthetic luciferase for the last common firefly ancestor exhibited green light caused by a spatial constraint on the luciferin molecule in enzyme, while fatty acyl-CoA synthetic activity, an original function of firefly luciferase, was diminished in exchange. All known firefly species are bioluminescent in the larvae, with a common ancestor arising approximately 100 million years ago. Combined, our findings propose that, within the mid-Cretaceous forest, the common ancestor of fireflies evolved green light luciferase via trade-off of the original function, which was likely aposematic warning display against nocturnal predation.
PubMed: 33268373
DOI: 10.1126/sciadv.abc5705
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.7 Å)
Structure validation

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