Metal-mediated self-assembly of protein superstructures: Influence of secondary interactions on protein oligomerization and aggregation
Metal-mediated self-assembly of protein superstructures: Influence of secondary interactions on protein oligomerization and aggregation
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DOI：
10.1021/ja8012177
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发表时间：
2008-05-14
影响因子：
15
通讯作者：
Tezcan, F. Akif
中科院分区：
文献类型：
--
作者：
Salgado, Eric N.;Lewis, Richard A.;Tezcan, F. Akif
我们以前已经证明，非自缔合蛋白质积木可以寡聚化，形成离散的超分子组装金属配位的控制下。我们在这里表明，二级相互作用（盐桥和氢键）可以在指导金属诱导的蛋白质自组装的关键。晶体学和流体动力学测量适当的N工程细胞色素cb（562）的变体，查明一个单一的盐桥精氨酸侧链的重要性，在确定蛋白质单体是否形成离散的锌诱导的四聚体复合物或异质性聚集体。通过金属配位和次级相互作用指导PPI的组合能力应提供构建复杂蛋白质超结构和选择性控制涉及蛋白质-蛋白质缔合反应的细胞过程所需的特异性。
We have previously demonstrated that non-self-associating protein building blocks can oligomerize to form discrete supramolecular assemblies under the control of metal coordination. We show here that secondary interactions (salt bridges and hydrogen bonds) can be critical in guiding the metal-induced self-assembly of proteins. Crystallographic and hydrodynamic measurements on appropriately N engineered cytochrome cb(562) variants pinpoint the importance of a single salt-bridging arginine side chain in determining whether the protein monomers form a discrete Zn-induced tetrameric complex or heterogeneous aggregates. The combined ability to direct PPIs through metal coordination and secondary interactions should provide the specificity required for the construction of complex protein superstructures and the selective control of cellular processes that involve protein-protein association reactions.