La cage aux fold: asymmetry in the crystal structure of GroEL-GroES-(ADP)7.
The structure of the molecular chaperone GroEL from Escherichia coli in complex with GroES and seven ADP molecules has recently been reported to 3 A resolution. The structure illustrates how the cavity of GroEL is converted from a hydrophobic environment, suitable for binding unfolded polypeptides, to a much larger hydrophilic environment suitable for refolding proteins.
Harrison
C J
CJ
Laboratories of Molecular Biophysics, Howard Hughes Medical Institute, Rockefeller University, NY 10021, USA. harrice@rockvax.rockefeller.edu
D000244:Adenosine Diphosphate / Q000737:chemistry* / Q000378:metabolism; D018835:Chaperonin 10 / Q000737:chemistry* / Q000378:metabolism; D018834:Chaperonin 60 / Q000737:chemistry* / Q000378:metabolism; D004926:Escherichia coli / Q000737:chemistry*; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding
D018835:Chaperonin 10; D018834:Chaperonin 60; D000244:Adenosine Diphosphate