Journal
CELL
Volume 149, Issue 1, Pages 113-123Publisher
CELL PRESS
DOI: 10.1016/j.cell.2012.02.047
Keywords
-
Categories
Funding
- National Institutes of Health though the National Center for Research Resources at Crystallography, Department of Biological Sciences and ISMB, Birkbeck College [RR017573]
- Wellcome Trust [070776, 089050]
- BBSRC
- MRC [G0600084]
- Human Frontier Science Program [RGY0079/2009-C]
- MRC [G0600084] Funding Source: UKRI
- Medical Research Council [G0600084] Funding Source: researchfish
Ask authors/readers for more resources
The chaperonin GroEL assists the folding of nascent or stress-denatured polypeptides by actions of binding and encapsulation. ATP binding initiates a series of conformational changes triggering the association of the cochaperonin GroES, followed by further large movements that eject the substrate polypeptide from hydrophobic binding sites into a GroES-capped, hydrophilic folding chamber. We used cryo-electron microscopy, statistical analysis, and flexible fitting to resolve a set of distinct GroEL-ATP conformations that can be ordered into a trajectory of domain rotation and elevation. The initial conformations are likely to be the ones that capture polypeptide substrate. Then the binding domains extend radially to separate from each other but maintain their binding surfaces facing the cavity, potentially exerting mechanical force upon kinetically trapped, misfolded substrates. The extended conformation also provides a potential docking site for GroES, to trigger the final, 100 degrees domain rotation constituting the power stroke that ejects substrate into the folding chamber.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available