The crystal structure of the bacterial chaperonin GroEL at 2.8 A.

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.

journal_name

Nature

journal_title

Nature

authors

Braig K,Otwinowski Z,Hegde R,Boisvert DC,Joachimiak A,Horwich AL,Sigler PB

doi

10.1038/371578a0

subject

Has Abstract

pub_date

1994-10-13 00:00:00

pages

578-86

issue

6498

eissn

0028-0836

issn

1476-4687

journal_volume

371

pub_type

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