The crystal structure of the GroES co-chaperonin at 2.8 A resolution

Nature. 1996 Jan 4;379(6560):37-45. doi: 10.1038/379037a0.


The GroES heptamer forms a dome, approximately 75 A in diameter and 30 A high, with an 8 A orifice in the centre of its roof. The 'mobile loop' segment, previously identified as a GroEL binding determinant, is disordered in the crystal structure in six subunits; the single well-ordered copy extends from the bottom outer rim of the GroES dome, suggesting that the cavity within the dome is continuous with the polypeptide binding chamber of GroEL in the chaperonin complex.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Chaperonin 10 / chemistry*
  • Chaperonin 10 / physiology
  • Computer Graphics
  • Crystallography, X-Ray
  • Molecular Sequence Data
  • Protein Conformation
  • Protein Folding
  • Protein Structure, Secondary


  • Chaperonin 10