Protein folding in the central cavity of the GroEL-GroES chaperonin complex

Nature. 1996 Feb 1;379(6564):420-6. doi: 10.1038/379420a0.

Abstract

The chaperonin GroEL is able to mediate protein folding in its central cavity. GroEL-bound dihydrofolate reductase assumes its native conformation when the GroES cofactor caps one end of the GroEL cylinder, thereby discharging the unfolded polypeptide into an enclosed cage. Folded dihydrofolate reductase emerges upon ATP-dependent GroES release. Other proteins, such as rhodanese, may leave GroEL after having attained a conformation that is committed to fold. Incompletely folded polypeptide rebinds to GroEL, resulting in structural rearrangement for another folding trial in the chaperonin cavity.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Chaperonin 60 / physiology*
  • Methotrexate
  • Mice
  • Models, Chemical
  • Molecular Sequence Data
  • Protein Conformation
  • Protein Folding*
  • Tetrahydrofolate Dehydrogenase / physiology*
  • Thiosulfate Sulfurtransferase / physiology

Substances

  • Chaperonin 60
  • Tetrahydrofolate Dehydrogenase
  • Thiosulfate Sulfurtransferase
  • Methotrexate