Empirical and computational design of iron-sulfur cluster proteins
Empirical and computational design of iron-sulfur cluster proteins
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DOI：
10.1016/j.bbabio.2012.02.001
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发表时间：
2012-08-01
影响因子：
4.3
通讯作者：
Noy, Dror
中科院分区：
文献类型：
--
作者：
Grzyb, Joanna;Xu, Fei;Noy, Dror
在这里，我们比较了两种蛋白质设计方法。一种计算方法被用于设计的卷曲螺旋铁硫蛋白，CCIS，作为一个四螺旋束结合铁硫簇在其疏水性核心。实验方法用于设计氧化还原链模型。RCM为四螺旋束，在环内组装铁硫簇，在其疏水核心的中间组装一个血红素。我们证明，这两种方式的设计产生了所需的蛋白质的二级结构和辅因子组装。然而，这两种方法在预测结合辅因子存在下的构象变化、控制低聚倾向和稳定还原状态下的结合铁硫簇方面仍有很大的改进空间。从这两种方式的设计和未来的发展方向的经验教训进行了讨论。这篇文章是特刊的一部分，题为：光合作用研究的可持续性：从自然到人工。(C)2012爱思唯尔有限公司版权所有。
Here, we compare two approaches of protein design. A computational approach was used in the design of the coiled-coil iron-sulfur protein, CCIS, as a four helix bundle binding an iron-sulfur cluster within its hydrophobic core. An empirical approach was used for designing the redox-chain maquette. RCM as a four-helix bundle assembling iron-sulfur clusters within loops and one heme in the middle of its hydrophobic core. We demonstrate that both ways of design yielded the desired proteins in terms of secondary structure and cofactors assembly. Both approaches, however, still have much to improve in predicting conformational changes in the presence of bound cofactors, controlling oligomerization tendency and stabilizing the bound iron-sulfur clusters in the reduced state. Lessons from both ways of design and future directions of development are discussed. This article is part of a Special Issue entitled: Photosynthesis Research for Sustainability: from Natural to Artificial. (C) 2012 Elsevier B.V. All rights reserved.