Sandbox 167

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== Introduction ==
== Introduction ==
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Japanese firefly. <ref name="main">PMID:15665092</ref>
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Bioluminescence is utilized by fireflies during mate selection. (sci name here) is <ref name="main">PMID:15665092</ref>
== Structure ==
== Structure ==
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Structure of japanese firefly luciferase.<ref name="main" />. The β-barrel structure actually has some homology with the human muscle fatty acid binding protein (m-FABP, pdb= 1HMT).
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Structure of japanese firefly luciferase.<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 23:10, 6 August 2010

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 fireflies during mate selection. (sci name here) is [1]

Structure

Structure of japanese firefly luciferase.[1].

Image:IMAGENAMEHERE.jpg
Figure 1: Caption for figure 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.




Related Links

Pymol molecular viewer

Protein Data Bank file on 1VPR

NCBI protein entry on P. lunula luciferase

References

  1. 1.0 1.1 Schultz LW, Liu L, Cegielski M, Hastings JW. Crystal structure of a pH-regulated luciferase catalyzing the bioluminescent oxidation of an open tetrapyrrole. Proc Natl Acad Sci U S A. 2005 Feb 1;102(5):1378-83. Epub 2005 Jan 21. PMID:15665092
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