PMID:7935790

Citation	Braig, K, Otwinowski, Z, Hegde, R, Boisvert, DC, Joachimiak, A, Horwich, AL and Sigler, PB (1994) The crystal structure of the bacterial chaperonin GroEL at 2.8 A. Nature 371:578-86
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.
Links	PubMed Online version:10.1038/371578a0
Keywords	Amino Acid Sequence; Chaperonin 60/chemistry; Computer Graphics; Crystallography, X-Ray; Escherichia coli; Models, Molecular; Molecular Sequence Data; Protein Conformation
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