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1: Nature. 1994 Oct 13;371(6498):578-86.Click here to read Links
Comment in:
Nature. 1994 Oct 13;371(6498):557-9.

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

Braig K, Otwinowski Z, Hegde R, Boisvert DC, Joachimiak A, Horwich AL, Sigler PB.

Department 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.

PMID: 7935790 [PubMed - indexed for MEDLINE]

Structures reported by this article