The lid that shapes the pot: structure and function of the chaperonin GroES.
The structure of GroES reveals a potential for instability at odds with the idea of a fixed ring whose only flexible regions are at the outer edges. The importance of GroES in chaperoned protein folding is highlighted by evidence that folding substrates are transiently enclosed under the GroES cap.
Saibil
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Department of Crystallography, Birkbeck College, London.
D000255:Adenosine Triphosphate / Q000378:metabolism; D001665:Binding Sites; D018835:Chaperonin 10 / Q000737:chemistry* / Q000378:metabolism*; D018834:Chaperonin 60 / Q000378:metabolism; D018833:Chaperonins / Q000737:chemistry / Q000378:metabolism; D006133:Growth Substances / Q000378:metabolism; D008958:Models, Molecular; D010455:Peptides / Q000378:metabolism; D011487:Protein Conformation; D017510:Protein Folding
D018835:Chaperonin 10; D018834:Chaperonin 60; D006133:Growth Substances; D010455:Peptides; D000255:Adenosine Triphosphate; D018833:Chaperonins