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细菌伴侣蛋白GroEL在2.8埃时的晶体结构。

The crystal structure of the bacterial chaperonin GroEL at 2.8 A.

作者信息

Braig K, Otwinowski Z, Hegde R, Boisvert D C, Joachimiak A, Horwich A L, Sigler P B

机构信息

Department of Genetics, Yale University School of Medicine, Boyer Center, New Haven, Connecticut 06510.

出版信息

Nature. 1994 Oct 13;371(6498):578-86. doi: 10.1038/371578a0.

DOI:10.1038/371578a0
PMID:7935790
Abstract

The crystal structure of Escherichia coli GroEL shows a porous cylinder of 14 subunits made of two nearly 7-fold rotationally symmetrical rings stacked back-to-back with dyad symmetry. The subunits consist of three domains: a large equatorial domain that forms the foundation of the assembly at its waist and holds the rings together; a large loosely structured apical domain that forms the ends of the cylinder; and a small slender intermediate domain that connects the two, creating side windows. The three-dimensional structure places most of the mutationally defined functional sites on the channel walls and its outward invaginations, and at the ends of the cylinder.

摘要

大肠杆菌GroEL的晶体结构显示为一个由14个亚基组成的多孔圆柱体,这14个亚基由两个近乎7次旋转对称的环背靠背堆叠而成,具有二重对称性。这些亚基由三个结构域组成:一个大的赤道结构域,它在腰部形成装配的基础并将两个环连接在一起;一个大的结构松散的顶端结构域,它形成圆柱体的两端;以及一个小的细长中间结构域,它连接前两者,形成侧面窗口。三维结构将大多数通过突变定义的功能位点置于通道壁及其向外的凹陷处,以及圆柱体的末端。

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