通过金属配位控制蛋白质寡聚化对称性：通过铜（II）和镍（II）配位形成C2和C3对称聚集体。
Control of protein oligomerization symmetry by metal coordination: C2 and C3 symmetrical assemblies through Cu(II) and Ni(II) coordination.
作者信息
Salgado Eric N, Lewis Richard A, Mossin Susanne, Rheingold Arnold L, Tezcan F Akif
机构信息
Department of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, La Jolla, California 92093, USA.
出版信息
Inorg Chem. 2009 Apr 6;48(7):2726-8. doi: 10.1021/ic9001237.
Abstract
We describe the metal-dependent self-assembly of symmetrical protein homooligomers from protein building blocks that feature appropriately engineered metal-chelating motifs on their surfaces. Crystallographic studies indicate that the same four-helix-bundle protein construct, MBPC-1, can self-assemble into C(2) and C(3) symmetrical assemblies dictated by Cu(II) and Ni(II) coordination, respectively. The symmetry inherent in metal coordination can thus be directly applied to biological self-assembly.
摘要
我们描述了由蛋白质构建块形成的对称蛋白质同聚体的金属依赖性自组装，这些构建块在其表面具有经过适当工程设计的金属螯合基序。晶体学研究表明，相同的四螺旋束蛋白构建体MBPC-1可以分别自组装成由Cu(II)和Ni(II)配位决定的C(2)和C(3)对称组装体。因此，金属配位中固有的对称性可以直接应用于生物自组装。
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