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Construction of a Triangle‐Shaped Trimer and a Tetrahedron Using an α‐Helix‐Inserted Circular Permutant of Cytochrome c555
Chemistry - An Asian Journal ( IF 3.5 ) Pub Date : 2018-03-15 , DOI: 10.1002/asia.201800252
Akiya Oda 1 , Satoshi Nagao 1 , Masaru Yamanaka 1 , Ikki Ueda 1 , Hiroki Watanabe 2 , Takayuki Uchihashi 2 , Naoki Shibata 3, 4 , Yoshiki Higuchi 3, 4 , Shun Hirota 1
Affiliation  

Highly‐ordered protein structures have gained interest for future uses for biomaterials. Herein, we constructed a building block protein (BBP) by the circular permutation of the hyperthermostable Aquifex aeolicus cytochrome (cyt) c555, and assembled BBP into a triangle‐shaped trimer and a tetrahedron. The angle of the intermolecular interactions of BBP was controlled by cleaving the domain‐swapping hinge loop of cyt c555 and connecting the original N‐ and C‐terminal α‐helices with an α‐helical linker. We obtained BBP oligomers up to ≈40 mers, with a relatively large amount of trimers. According to the X‐ray crystallographic analysis of the BBP trimer, the N‐terminal region of one BBP molecule interacted intermolecularly with the C‐terminal region of another BBP molecule, resulting in a triangle‐shaped structure with an edge length of 68 Å. Additionally, four trimers assembled into a unique tetrahedron in the crystal. These results demonstrate that the circular permutation connecting the original N‐ and C‐terminal α‐helices with an α‐helical linker may be useful for constructing organized protein structures.

中文翻译:

利用细胞色素c555的α-螺旋插入的圆形置换构建三角形的三聚体和四面体

高度有序的蛋白质结构引起了人们对生物材料未来用途的兴趣。在这里,我们通过超耐热的Aquifex aeolicus细胞色素(cyt)c 555的圆形排列构建了构件蛋白(BBP),然后将BBP组装成三角形的三聚体和四面体。通过裂解cyt c 555的域交换铰链环来控制BBP的分子间相互作用的角度并将原始的N端和C端α螺旋与一个α螺旋接头连接。我们获得了BBP寡聚体,其含量高达约40聚体,且三聚体的含量相对较高。根据BBP三聚体的X射线晶体学分析,一个BBP分子的N末端区域与另一个BBP分子的C末端区域发生了分子间相互作用,形成了边长为68Å的三角形结构。此外,四个三聚体在晶体中组装成一个独特的四面体。这些结果表明,将原始的N末端和C末端的α螺旋与一个α螺旋接头连接起来的圆形排列对于构建有组织的蛋白质结构可能是有用的。
更新日期:2018-03-15
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