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Updated: Aug 19, 2026

From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins
Published on: July 4, 2016
The crystal structure of the bacterial chaperonin GroEL at 2.8 A
K Braig1, Z Otwinowski, R Hegde
1Department of Genetics, Yale University School of Medicine, Boyer Center, New Haven, Connecticut 06510.
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.
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