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 mutation-ally defined functional sites on the channel walls and its outward imaginations, and at the ends of the cylinder.
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Braig, K., Otwinowski, Z., Hegde, R. et al. The crystal structure of the bacterial chaperonln GroEL at 2.8 Å. Nature 371, 578–586 (1994). https://doi.org/10.1038/371578a0
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DOI: https://doi.org/10.1038/371578a0
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