Sandbox 167

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== Structure ==
== Structure ==
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Chemically, L. cruciata luciferase is similiar to aminoacyl-tRNA synthetases, so much that DLSA, an analog of a potent inhibitor of said synthetases was used to help solve it's structure. While the primary sequence of both proteins is similiar, the binding affinity of the luciferase for this inhibitor also suggests that the first part of the luciferase reaction might share a similiar mechanism as well. <ref name="structure" PMID:16541080 />.
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Generally, firefly luciferases have some similarities with Acyl-CoA ligases and some peptide synthetases despite having different cellular effects. In fixing the structure of L. cruciata luciferase, the analog of a potent aminoacyl-tRNA synthetases (DLSA) was successfuly utilized to represent a stable oxyluciferin intermediate.<ref name="structure">PMID:16541080 </ref>.
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The active site for this luciferase 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" />.
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The DLSA occupied the active site of the luciferase, which 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="structure" />.
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[[Image:2d1s active site with ILE288.jpg | thumb |none | upright=3.0 | Figure 1: Caption for figure 1]]
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Notes about the image
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Second image
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Notes about the image
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== Luciferase Reaction ==
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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.
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[[Image:2d1s active site with ILE288.jpg | thumb |none | upright=3.0 | Figure 1: PYMOL image of 2D1S highlighting active site and Ile288, putatively identified in hydrophobic control of bioluminescent colour.]]
== Related Links ==
== Related Links ==
[http://www.pymol.org/ Pymol molecular viewer]
[http://www.pymol.org/ Pymol molecular viewer]
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[http://www.pdb.org/pdb/explore/explore.do?structureId=1VPR Protein Data Bank file on 1VPR]
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[http://www.pdb.org/pdb/explore/explore.do?structureId=2D1S Protein Data Bank file on 2D1S]
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[http://www.ncbi.nlm.nih.gov/protein/ABO61076.1?ordinalpos=1&itool=EntrezSystem2.PEntrez.Sequence.Sequence_ResultsPanel.Sequence_RVDocSum NCBI protein entry on ''P. lunula'' luciferase]
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[http://www.ncbi.nlm.nih.gov/protein/CAA59282.1 NCBI protein entry on ''Photinus pyralis'' luciferase, the american firefly]
== References ==
== References ==
<references />
<references />

Current revision

PDB ID 2d1s

Drag the structure with the mouse to rotate
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




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 firefly luciferase from Luciola cruciata is one of many commonly utilized for such purposes as such as sensing cellular ATP levels or visualizing the effects of a promoter sequence, among several others.

Structure

Generally, firefly luciferases have some similarities with Acyl-CoA ligases and some peptide synthetases despite having different cellular effects. In fixing the structure of L. cruciata luciferase, the analog of a potent aminoacyl-tRNA synthetases (DLSA) was successfuly utilized to represent a stable oxyluciferin intermediate.[2]. The DLSA occupied the active site of the luciferase, which 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. [2].

Figure 1: PYMOL image of 2D1S highlighting active site and Ile288, putatively identified in hydrophobic control of bioluminescent colour.
Figure 1: PYMOL image of 2D1S highlighting active site and Ile288, putatively identified in hydrophobic control of bioluminescent colour.

Related Links

Pymol molecular viewer

Protein Data Bank file on 2D1S

NCBI protein entry on Photinus pyralis luciferase, the american firefly

References

  1. ↑ Suzuki H, Sato Y, Fujiyama S, Ohba N. Biochemical systematics of Japanese fireflies of the subfamily Luciolinae and their flash communication systems. Biochem Genet. 1996 Jun;34(5-6):191-200. PMID:8813052
  2. ↑ 2.0 2.1 Nakatsu T, Ichiyama S, Hiratake J, Saldanha A, Kobashi N, Sakata K, Kato H. Structural basis for the spectral difference in luciferase bioluminescence. Nature. 2006 Mar 16;440(7082):372-6. PMID:16541080 doi:10.1038/nature04542
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