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Int J Biol Macromol. 2018 Oct 15;118(Pt A):671-675. doi: 10.1016/j.ijbiomac.2018.06.120. Epub 2018 Jun 27.

A two-domain folding intermediate of RuBisCO in complex with the GroEL chaperonin.

Author information

1
Crystallography and Institute of Structural and Molecular Biology, Birkbeck College London, Malet Street, London, WC1E 7HX, UK.
2
Department of Genetics, Yale University School of Medicine, Boyer Center, 295 Congress Avenue, New Haven, CT 06510, USA.
3
Department of Genetics, Yale University School of Medicine, Boyer Center, 295 Congress Avenue, New Haven, CT 06510, USA; Howard Hughes Medical Institute, Yale University School of Medicine, 295 Congress Avenue, New Haven, CT 06510, USA.
4
Crystallography and Institute of Structural and Molecular Biology, Birkbeck College London, Malet Street, London, WC1E 7HX, UK. Electronic address: h.saibil@mail.cryst.bbk.ac.uk.

Abstract

The chaperonins (GroEL and GroES in Escherichia coli) are ubiquitous molecular chaperones that assist a subset of essential substrate proteins to undergo productive folding to the native state. Using single particle cryo EM and image processing we have examined complexes of E. coli GroEL with the stringently GroE-dependent substrate enzyme RuBisCO from Rhodospirillum rubrum. Here we present snapshots of non-native RuBisCO - GroEL complexes. We observe two distinct substrate densities in the binary complex reminiscent of the two-domain structure of the RuBisCO subunit, so that this may represent a captured form of an early folding intermediate. The occupancy of the complex is consistent with the negative cooperativity of GroEL with respect to substrate binding, in accordance with earlier mass spectroscopy studies.

KEYWORDS:

Chaperonin; GroEL; Non-native protein; Protein folding; RuBisCO; Single particle cryo-EM

PMID:
29959019
PMCID:
PMC6096091
DOI:
10.1016/j.ijbiomac.2018.06.120
[Indexed for MEDLINE]
Free PMC Article

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