Chaperonin complex with a newly folded protein encapsulated in the folding chamber

D. K. Clare, P. J. Bakkes, H. van Heerikhuizen, S. M. van der Vies () and H. R. Saibil ()
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D. K. Clare: Birkbeck College, Malet Street, London WC1E 7HX, UK
P. J. Bakkes: VU University Medical Center, De Boelelaan 1117, 1081 HV Amsterdam, The Netherlands
H. van Heerikhuizen: VU University Medical Center, De Boelelaan 1117, 1081 HV Amsterdam, The Netherlands
S. M. van der Vies: VU University Medical Center, De Boelelaan 1117, 1081 HV Amsterdam, The Netherlands
H. R. Saibil: Birkbeck College, Malet Street, London WC1E 7HX, UK

Nature, 2009, vol. 457, issue 7225, 107-110

Abstract: Chaperonins: structure of a newly folded protein In Escherichia coli the chaperonins GroEL and GroES form a double-ring complex that binds and folds nascent or unfolded proteins. The T4 bacteriophage has its own version of GroES, gp31, that forms a taller folding chamber to fold the major virus capsid protein, gp23. Clare et al. present the structure of gp23–chaperonin complexes showing gp23 encapsulated in the folding chamber. The folding chamber is distorted in order to enclose a large substrate. This is the first study to present an image of a newly folded protein just before its release from the GroEL folding chamber.

Date: 2009
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DOI: 10.1038/nature07479

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