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Article
Nature 371, 578 - 586 (13 October 1994); doi:10.1038/371578a0

The crystal structure of the bacterial chaperonln GroEL at 2.8 Å

Kerstin Braig*, Zbyszek Otwinowski§, Rashmi Hegde§, David C. Boisvert*, Andrzej Joachimiak§, Arthur L. Horwich* & Paul B. Sigler

*Department of Genetics Department of Molecular Biophysics and Biochemistry andHoward Hughes Medical Institute, Yale University School of Medicine, Boyer Center, 295 Congress Avenue, New Haven, Connecticut 06510,USA
§Present addresses: Department of Biochemistry, University of Texas Southwestern Medical Center, 5323 Harry Mines Blvd, Dallas, Texas 75235-9038, USA (Z.O.); Skirball Institute of Biomolecular Medicine, New York University Medical Center, New York, New York 10016, USA (R.H.); Argonne National Laboratory, 9700 Cass Avenue, Argonne, Illinois 60439-4833, USA (A.J.).
To whom correspondence should be addressed.

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 mutation-ally defined functional sites on the channel walls and its outward imaginations, and at the ends of the cylinder.

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