Helen
Saibil, Shaoxia Chen, Alan Roseman (now at MRC LMB, Cambridge), Helen White, Neil
Ranson, Jose L. Jimenez, Guy Schoehn, Steve Burston (on his way to Bristol)
Supported by Birkbeck College, The Wellcome Trust and the BBSRC
GroEL, GroEL-ATP and
GroEL-GroES-ATP
Our previous work on cryo EM of chaperonins was published in Chen et al, (1994)
Nature 371, 261-264. This work was part of a collaboration with Tony Clarke, Steve Burston
and Neil Ranson.
More recent work, published in Cell, includes movies of the GroEL ATPase cycle. These can be obtained either from the Cell Web site or from here.
The
chaperonin ATPase cycle: mechanism of allosteric switching and movements of
substrate-binding domains in GroEL
Alan Roseman, Shaoxia Chen, Helen White, Kerstin Braig* and Helen Saibil
Department of Crystallography, Birkbeck College, Malet St, London WC1E 7HX, UK
*Howard Hughes Medical Institute, Yale University School of Medicine; Present address: MRC
Laboratory of Molecular Biology, Cambridge CB2 2QH
Cell 87, 241-251 (1996) (Abstract)
GroEL-nucleotide structures at 30 Å resolution
GroEL-GroES complexes at 30 Å resolution
Atomic structure of GroEL inter-ring contacts (blue/red charge pairs), the
alpha-helix (green) connecting the front contact to the ATP binding site and the bound ATP
(lilac), fitted into GroEL-ADP and ATP structures from cryo EM (white wire mesh surfaces).
Click on the image for bigger version of both structures.
Movies of the GroEL ATPase cycle
White, H., Chen, S., Roseman, A., Yifrach, O., Horovitz, A. & Saibil, H. (1997) Structural basis of allosteric changes in the GroEL mutant Arg197Ala. Nature Struct. Biol. 4, 690-694.
Book Chapter
H. Saibil, Chaperonin Structure and Conformational Changes, inThe Chaperonins, R.J.Ellis, Ed., Academic Press 1996. Reproduced by permission of Academic Press.