Sandbox 167
From Proteopedia
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| 2d1s, resolution 1.30Å () | |||||||||
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| Ligands: | , | ||||||||
| Non-Standard Residues: | |||||||||
| Activity: | Photinus-luciferin 4-monooxygenase (ATP-hydrolyzing), with EC number 1.13.12.7 | ||||||||
| Related: | 2d1r, 2d1t | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB, TOPSAN | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Contents |
Introduction
Bioluminescence is utilized by several nocturnal japanese firely species during mate selection, with males and females illuminating equally. Several common signals appear to be used to communicate everything from "male awaiting a mate" to "female here". [1] While the reaction is quite similiar to that of other bioluminescent luciferases, firefly luciferase has a unique structure in both the protein and luciferin required to produce the bioluminescence. In research, the luciferase reaction is utilized for many purposes, such as sensing cellular ATP levels or visualizing the effects of a promoter.
Structure
Structure of japanese firefly luciferase.[1].
Notes about the image
Second image
Notes about the image
Luciferase Reaction
Typically, luciferases produce light through a high energy complex with a luciferin cofactor, and Mg-ATP. While the reaction appears to be similiar across all luciferases, species-variants in the luciferin and luciferase structure, and the exact chemical reaction exist.
Related Links
Protein Data Bank file on 1VPR
NCBI protein entry on P. lunula luciferase
