2d1t

File:2d1t.gif

spinqualitylabelsall models 2d1t, resolution 1.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of the thermostable Japanese Firefly Luciferase red-color emission S286N mutant complexed with High-energy intermediate analogue

OverviewOverview

Fireflies communicate with each other by emitting yellow-green to, yellow-orange brilliant light. The bioluminescence reaction, which uses, luciferin, Mg-ATP and molecular oxygen to yield an electronically excited, oxyluciferin species, is carried out by the enzyme luciferase. Visible, light is emitted during relaxation of excited oxyluciferin to its ground, state. The high quantum yield of the luciferin/luciferase reaction and the, change in bioluminescence colour caused by subtle structural differences, in luciferase have attracted much research interest. In fact, a single, amino acid substitution in luciferase changes the emission colour from, yellow-green to red. Although the crystal structure of luciferase from the, North American firefly (Photinus pyralis) has been described, the detailed, mechanism for the bioluminescence colour change is still unclear. Here we, report the crystal structures of wild-type and red mutant (S286N), luciferases from the Japanese Genji-botaru (Luciola cruciata) in complex, with a high-energy intermediate analogue, 5'-O-[N-(dehydroluciferyl)-sulfamoyl]adenosine (DLSA). Comparing these, structures to those of the wild-type luciferase complexed with AMP plus, oxyluciferin (products) reveals a significant conformational change in the, wild-type enzyme but not in the red mutant. This conformational change, involves movement of the hydrophobic side chain of Ile 288 towards the, benzothiazole ring of DLSA. Our results indicate that the degree of, molecular rigidity of the excited state of oxyluciferin, which is, controlled by a transient movement of Ile 288, determines the colour of, bioluminescence during the emission reaction.

About this StructureAbout this Structure

2D1T is a Single protein structure of sequence from Luciola cruciata with CL and SLU as ligands. The following page contains interesting information on the relation of 2D1T with [Luciferase]. Active as Photinus-luciferin 4-monooxygenase (ATP-hydrolyzing), with EC number 1.13.12.7 Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for the spectral difference in luciferase bioluminescence., Nakatsu T, Ichiyama S, Hiratake J, Saldanha A, Kobashi N, Sakata K, Kato H, Nature. 2006 Mar 16;440(7082):372-6. PMID:16541080

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