Sandbox 167: Difference between revisions
James Jones (talk | contribs) |
James Jones (talk | contribs) |
||
| Line 8: | Line 8: | ||
== Structure == | == Structure == | ||
The | The active site for 2D1S lies within a central area of the protein, and is composed of an α-helix (residues 248-260) and four short β-sheets (residues 286-289, 313-316, 339-342 and 351-353. Ile288 has been implicated as an important residue in determining the hydrophobicity of the active site environment, and through orientation of the product oxyluciferin, the bioluminescent colour. <ref name="main" />. | ||
[[Image:IMAGENAMEHERE.jpg | thumb |none | upright=3.0 | Figure 1: Caption for figure 1]] | [[Image:IMAGENAMEHERE.jpg | thumb |none | upright=3.0 | Figure 1: Caption for figure 1]] | ||
Revision as of 01:45, 19 August 2010
| |||||||||
| 2d1s, resolution 1.30Å () | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||||
| Non-Standard Residues: | |||||||||
| Activity: | Photinus-luciferin 4-monooxygenase (ATP-hydrolyzing), with EC number 1.13.12.7 | ||||||||
| Related: | 2d1r, 2d1t | ||||||||
| |||||||||
| |||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB, TOPSAN | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
IntroductionIntroduction
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.
StructureStructure
The active site for 2D1S lies within a central area of the protein, and is composed of an α-helix (residues 248-260) and four short β-sheets (residues 286-289, 313-316, 339-342 and 351-353. Ile288 has been implicated as an important residue in determining the hydrophobicity of the active site environment, and through orientation of the product oxyluciferin, the bioluminescent colour. [1].
Notes about the image
Second image
Notes about the image
Luciferase ReactionLuciferase 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 LinksRelated Links
Protein Data Bank file on 1VPR
NCBI protein entry on P. lunula luciferase