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Nature. 1994 Oct 13;371(6498):578-86.

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

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  • 1Department of Genetics, Yale University School of Medicine, Boyer Center, New Haven, Connecticut 06510.


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.

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