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Braig K, et al.  (1994) The crystal structure of the bacterial chaperonin GroEL at 2.8 A. Nature 371(6498):578-86

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.

Status: Published

Type: Journal Article

PubMed ID: 7935790

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Braig K Otwinowski Z Hegde R Boisvert DC Joachimiak A Horwich AL Sigler PB Papers in SGD Colleagues in SGD PubMed Google Scholar

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