Controlling protein-protein interactions through metal coordination: Assembly of a 16-helix bundle protein
Controlling protein-protein interactions through metal coordination: Assembly of a 16-helix bundle protein
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DOI：
10.1021/ja075261o
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发表时间：
2007-11-07
影响因子：
15
通讯作者：
Tezcan, F. Alkif
中科院分区：
文献类型：
--
作者：
Salgado, Eric N.;Faraone-Mennella, Jasmin;Tezcan, F. Alkif
蛋白质-蛋白质相互作用（PPI）的预测，设计和控制仍然是巨大的挑战，尽管最近的进展。在这里，我们描述了PPIs的化学控制，通过使用金属配位，它规避了PPIs的要求，广泛的弱相互作用分布在一个大的表面。一种非自缔合四束蛋白，细胞色素cb（562），与适当的工程金属结合基序自组装成一个16螺旋四级结构后，加入等摩尔锌。组装的晶体结构，结合PFG扩散NMR和沉降速度实验，表明细胞色素cb（562）的寡聚化性质完全由金属配位决定，而没有来自特定PPI的显著热力学偏差。
The prediction, design, and control of protein-protein interactions (PPIs) remain great challenges despite recent advances. Here we describe the chemical control of PPIs through the use of metal coordination, which circumvents the requirement of PPIs for an extensive set of weak interactions spread over a large surface. A non-self-associating four-bundle protein, cytochrome cb (562), with appropriately engineered metal-binding motifs self-assembles to a 16-helix quaternary structure upon addition of equimolar Zn. The crystal structure of the assembly, combined with PFG diffusion NMR and sedimentation velocity experiments, indicates that the oligomerization properties of cytochrome cb (562) are governed entirely by metal coordination without significant thermodynamic bias from specific PPIs.