The crystal structure of the bacterial chaperonin GroEL at 2.8 A.
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.
Braig
K
K
Department of Genetics, Yale University School of Medicine, Boyer Center, New Haven, Connecticut 06510.
Otwinowski
Z
Z
Hegde
R
R
Boisvert
D C
DC
Joachimiak
A
A
Horwich
A L
AL
Sigler
P B
PB
D000595:Amino Acid Sequence; D018834:Chaperonin 60 / Q000737:chemistry*; D003196:Computer Graphics; D018360:Crystallography, X-Ray; D004926:Escherichia coli; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation
D018834:Chaperonin 60