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Structural basis for the spectral difference in luciferase bioluminescence.

机译：荧光素酶生物发光光谱差异的结构基础。

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摘要

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.
机译：萤火虫通过发出黄绿色至黄橙色的明亮光来相互交流。利用荧光素酶进行利用荧光素，Mg-ATP和分子氧产生电子激发的氧化荧光素物质的生物发光反应。在激发的氧化萤光素松弛至其基态期间发射可见光。萤光素/萤光素酶反应的高量子产率以及萤光素酶的细微结构差异引起的生物发光颜色的变化吸引了许多研究兴趣。实际上，萤光素酶中的单个氨基酸取代将发射颜色从黄绿色变为红色。尽管已经描述了来自北美萤火虫（Photinus pyralis）的萤光素酶的晶体结构，但生物发光颜色变化的详细机制仍不清楚。在这里我们报告了来自日本源氏-botaru（Luciola cruciata）的野生型和红色突变体（S286N）荧光素酶的晶体结构，与高能中间类似物5'-O- [N-（dehydroluciferyl）-氨磺酰基混合腺苷（DLSA）。将这些结构与与AMP +氧化荧光素复合的野生型荧光素酶的结构进行比较（产品），发现野生型酶具有显着的构象变化，而红色突变体则没有。这种构象变化涉及Ile 288的疏水侧链向DLSA的苯并噻唑环的移动。我们的结果表明，受Ile 288瞬态运动控制的氧化荧光素激发态的分子刚性程度决定了发射反应过程中生物发光的颜色。

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