ArticleInternational journal of biological macromolecules2018
A two-domain folding intermediate of RuBisCO in complex with the GroEL chaperonin.
Article in International journal of biological macromolecules, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 15 citations in OpenAlex.
- Review
- Native Capillary Electrophoresis-Mass Spectrometry of Near 1 MDa Non-Covalent GroEL/GroES/Substrate Protein Complexes.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Structural basis of substrate progression through the bacterial chaperonin cycle.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Cryo-EM structures of GroEL:ESiScience · 2022Article
- Novel cryo-EM structure of an ADP-bound GroEL-GroES complex.Scientific reports · 2021Article
- A Long-Day Photoperiod and 6-Benzyladenine Promote Runner Formation through Upregulation of Soluble Sugar Content in Strawberry.International journal of molecular sciences · 2020Article
- Structural and functional analysis of the role of the chaperonin CCT in mTOR complex assembly.Nature communications · 2019Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
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.
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Registered trials
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