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

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.

SUBMITTER: Natesh R

PROVIDER: S-EPMC6096091 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature

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

Natesh Ramanathan R Clare Daniel K DK Farr George W GW Horwich Arthur L AL Saibil Helen R HR

International journal of biological macromolecules 20180627 Pt A

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 bina ...[more]

PMID: 29959019

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