Crystal structure of the Aequorea victoria green fluorescent protein
Crystal structure of the Aequorea victoria green fluorescent protein
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DOI：
10.1126/science.273.5280.1392
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发表时间：
1996-09-06
期刊：
影响因子：
56.9
通讯作者：
Remington, SJ
中科院分区：
文献类型：
--
作者：
Ormo, M;Cubitt, AB;Remington, SJ
来自太平洋西北部水母Aequorea维多利亚的绿色荧光蛋白（GFP）作为基因表达和基因产物定位的标记物引起了人们的强烈兴趣。发色团由Ser（65）（或Thr（65））-Tyr（66）-Gly（67）序列的自发环化和氧化产生，其形成和荧光发射都需要天然蛋白质折叠。Thr（65）GFP的结构已在1.9埃分辨率下确定，蛋白质折叠由具有同轴螺旋的11链β桶组成，其中发色团从中心螺旋形成。将与发色团相邻的一个残基Thr（203）定向诱变为Tyr或His导致显著红移的激发和发射最大值。
The green fluorescent protein (GFP) from the Pacific Northwest jellyfish Aequorea victoria has generated intense interest as a marker for gene expression and localization of gene products, The chromophore, resulting from the spontaneous cyclization and oxidation of the sequence -Ser(65) (or Thr(65))-Tyr(66)-Gly(67)-, requires the native protein fold for both formation and fluorescence emission. The structure of Thr(65) GFP has been determined at 1.9 angstrom resolution, The protein fold consists of an 11-stranded beta barrel with a coaxial helix, with the chromophore forming from the central helix. Directed mutagenesis of one residue adjacent to the chromophore, Thr(203), to Tyr or His results in significantly red-shifted excitation and emission maxima.