Light-Induced Rearrangement of the β5 Strand in the BLUF Photoreceptor SyPixD (Slr1694).

Light-Induced Rearrangement of the β5 Strand in the BLUF Photoreceptor SyPixD (Slr1694).
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BLUF 感光器 SyPixD (Slr1694) 中 β5 链的光诱导重排

DOI:
10.1021/acs.jpclett.5b02245
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发表时间:
2015
期刊:
The journal of physical chemistry letters
影响因子:
--
通讯作者:
Mathes T
Mathes T
中科院分区:
--
文献类型:
--
作者:
Mehlhorn J;Lindtner T;Richter F;Glaß K;Steinocher H;Beck S;Hegemann P;Kennis JTM ;Mathes T

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在使用FAD(BLUF)光感受器的蓝光传感器中,促进信号转导的结构变化以及在信号状态下黄素和蛋白质之间重排的氢键网络的稳定性仍然知之甚少。在这里,我们用同位素编辑的振动光谱和定点突变技术研究了SyPixD(Slr1694)中的一个半服务色氨酸残基。在信令状态下,形成了包含W91主链的β-Sheet结构,而W91吲哚侧链的环境没有明显变化。然而,W91的突变显著影响光适应状态的稳定性,这表明主干刚性而不是离散的侧链构象控制光适应状态的稳定性。在计算和结晶学模型的基础上,我们将这些变化解释为β2/β5相互作用的+1寄存器移位与未受影响的吲哚侧链构象,而不是先前根据X射线结构提出的伴随吲哚侧链翻转的+2寄存器移位。
The structural changes that facilitate signal transduction in blue light sensors using FAD (BLUF) photoreceptors and confer the stability of the rearranged hydrogen bond network between flavin and protein in the signaling state are still poorly understood. Here, we investigate a semiconserved Trp residue in SyPixD (Slr1694) by isotope-edited vibrational spectroscopy and site-directed mutagenesis. In the signaling state, a β-sheet structure involving the backbone of W91 is formed without apparent change of environment of the W91 indole side chain. Mutation of W91, however, significantly influences the stability of the light-adapted state, suggesting that backbone rigidity rather than discrete side-chain conformations govern the stability of the light-adapted state. On the basis of computational and crystallographic models, we interpret these changes as a +1 register shift of the β2/β5 interaction with an unaffected indole side-chain conformation, rather than a +2 register shift accompanied by an indole side-chain flip that was previously proposed on the basis of X-ray structures.
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期刊: The journal of physical chemistry. B
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影响因子: 3.7
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期刊:
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影响因子: 4.8
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