 |
|
Title
|
|
The crystal structure of the bacterial chaperonin GroEL at 2.8 A.
|
|
|
Authors
|
|
K.Braig,
Z.Otwinowski,
R.Hegde,
D.C.Boisvert,
A.Joachimiak,
A.L.Horwich,
P.B.Sigler.
|
|
|
Ref.
|
|
Nature, 1994,
371,
578-586.
|
|
|
PubMed id
|
|
|
|
|
|
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.
|
|
|
|