The crystal structure of the bacterial chaperonln GroEL at 2.8 Å

Kerstin Braig, Zbyszek Otwinowskl, Rashmi Hegde, David C. Boisvert, Andrzej Joachimiak, Arthur L. Horwich, Paul B. Sigler

Research output: Contribution to journalReview article

1139 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)578-586
Number of pages9
JournalNature
Volume371
Issue number6498
DOIs
StatePublished - 1994

ASJC Scopus subject areas

  • General

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    Braig, K., Otwinowskl, Z., Hegde, R., Boisvert, D. C., Joachimiak, A., Horwich, A. L., & Sigler, P. B. (1994). The crystal structure of the bacterial chaperonln GroEL at 2.8 Å. Nature, 371(6498), 578-586. https://doi.org/10.1038/371578a0