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首页> 外文期刊>Journal of Molecular Biology >Structural and functional dynamics of an integral membrane protein complex modulated by lipid headgroup charge
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Structural and functional dynamics of an integral membrane protein complex modulated by lipid headgroup charge

机译：通过脂质头组充电调节的整体膜蛋白复合物的结构和功能动态

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摘要

We have used membrane surface charge to modulate the structural dynamics of an integral membrane protein, phospholamban (PLB), and thereby its functional inhibition of the sarcoplasmic reticulum Ca-ATPase (SERCA). It was previously shown by electron paramagnetic resonance, in vesicles of neutral lipids, that the PLB cytoplasmic domain is in equilibrium between an ordered T state and a dynamically disordered R state and that phosphorylation of PLB increases the R state and relieves SERCA inhibition, suggesting that R is less inhibitory. Here, we sought to control the T/R equilibrium by an alternative means-varying the lipid headgroup charge, thus perturbing the electrostatic interaction of PLB's cationic cytoplasmic domain with the membrane surface. We resolved the T and R states not only by electron paramagnetic resonance in the absence of SERCA but also by time-resolved fluorescence resonance energy transfer from SERCA to PLB, thus probing directly the SERCA-PLB complex. Compared to neutral lipids, anionic lipids increased both the T population and SERCA inhibition, while cationic lipids had the opposite effects. In contrast to conventional models, decreased inhibition was not accompanied by decreased binding. We conclude that PLB binds to SERCA in two distinct structural states of the cytoplasmic domain: an inhibitory T state that interacts strongly with the membrane surface and a less inhibitory R state that interacts more strongly with the anionic SERCA cytoplasmic domain. Modulating membrane surface charge provides an effective way of investigating the correlation between structural dynamics and function of integral membrane proteins.
机译：我们已经使用膜表面电荷来调节整体膜蛋白，磷蛋白（PLB）的结构动态，从而其肌肉网状蛋白Ca-AtP酶（Serca）的功能抑制。以前通过电子顺磁共振所示，在中性脂质的囊泡中，PLB细胞质结构域在有序的T状态和动态无序的R状态之间处于平衡，并且PLB的磷酸化增加了R状态并减轻SERCA抑制，表明这一点r是较少的抑制作用。这里，我们试图通过替代方法改变脂质头组电荷来控制T / R平衡，从而扰乱PLB的阳离子细胞质结构域与膜表面的静电相互作用。我们不仅在没有SERCA的情况下通过电子顺磁共振解决而且通过从SERCA至PLB的时间分辨荧光共振能量转移，因此请直接探测SERCA-PLB复合物。与中性脂质相比，阴离子脂质增加了T群体和SERCA抑制，而阳离子脂质具有相反的效果。与常规模型相比，降低的抑制不伴随着减少的结合。我们得出结论，PLB在细胞质结构域的两个不同结构状态下与SERCA结合：抑制T状态，其与膜表面强烈相互作用，并且与阴离子SERCA细胞质结构域更强烈地相互作用的抑制性R状态。调制膜表面电荷提供了研究结构动力学和整体膜蛋白的功能之间的相关方法。

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  • 来源
    《Journal of Molecular Biology》 |2012年第5期|共11页
  • 作者

    LiJ.; JamesZ.M.; DongX.; KarimC.B.; ThomasD.D.;

  • 作者单位

    Department of Biochemistry Molecular Biology and Biophysics University of Minnesota 321 Church;

    Department of Biochemistry Molecular Biology and Biophysics University of Minnesota 321 Church;

    Department of Biochemistry Molecular Biology and Biophysics University of Minnesota 321 Church;

    Department of Biochemistry Molecular Biology and Biophysics University of Minnesota 321 Church;

    Department of Biochemistry Molecular Biology and Biophysics University of Minnesota 321 Church;

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  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类 分子生物学;
  • 关键词

    electrostatic interactions; EPR; FRET; phospholamban; SERCA;

    机译：静电相互作用;epr;fret;磷丹佛兰;serca;

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