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

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.

Pubmed ID: 8559246

Authors

  • Mayhew M
  • da Silva AC
  • Martin J
  • Erdjument-Bromage H
  • Tempst P
  • Hartl FU

Journal

Nature

Publication Data

February 1, 1996

Associated Grants

None

Mesh Terms

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