Antson A A, Dodson E J, Dodson G G
Department of Chemistry, University of York, UK.
Curr Opin Struct Biol. 1996 Apr;6(2):142-50. doi: 10.1016/s0959-440x(96)80067-4.
During 1994 and 1995, the structures of the serum amyloid P component, the bacterial chaperonin GroEL, the 20S proteasome, the bacterial light-harvesting complexes and the tryptophan operon RNA-binding attenuation protein have been determined. These structures all form circular assemblies in which the individual subunits are related by rotational symmetry. In most cases the circular organization generates a new biophysical property and a specific biological function which have presumably been selected by evolution.
在1994年和1995年期间,血清淀粉样蛋白P成分、细菌伴侣蛋白GroEL、20S蛋白酶体、细菌光捕获复合体以及色氨酸操纵子RNA结合衰减蛋白的结构已被确定。这些结构均形成环状聚集体,其中各个亚基通过旋转对称性相关联。在大多数情况下,这种环状结构产生了一种新的生物物理特性和特定的生物学功能,这些大概是经过进化选择的。