The crystal structure of the bacterial chaperonin GroEL at 2.8 A

Nature. 1994 Oct 13;371(6498):578-86. doi: 10.1038/371578a0.


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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Chaperonin 60 / chemistry*
  • Computer Graphics
  • Crystallography, X-Ray
  • Escherichia coli
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation


  • Chaperonin 60