ArticleNature structural & molecular biology2011
Crystal structure of a chaperone-bound assembly intermediate of form I Rubisco.
Article in Nature structural & molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 75 citations in OpenAlex.
- Machine learning-assisted directed evolution of plant Rubisco.Science advances · 2026Article
- Functional and structural insights into cyanobacterial COThe Plant journal : for cell and molecular biology · 2026Review
- High-Throughput Detection of Cyanobacterial Form I Rubisco Assembly.ACS synthetic biology · 2026Article
- Directed evolution of a plant Rubisco chaperone with altered client recognition.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Review
- Genome-Wide Analysis and Expression Profiling of SoybeanInternational journal of molecular sciences · 2024Article
- In Vivo Incorporation of Photoproteins into GroEL Chaperonin Retaining Major Structural and Functional Properties.Molecules (Basel, Switzerland) · 2023Article
- Structural insights into cyanobacterial RuBisCO assembly coordinated by two chaperones Raf1 and RbcX.Cell discovery · 2022Article
- A temporal gradient of cytonuclear coordination of chaperonins and chaperones during RuBisCo biogenesis in allopolyploid plants.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- GroEL-A Versatile Chaperone for Engineering and a Plethora of Applications.Biomolecules · 2022Review
- Transcriptome-Wide Gene Expression Plasticity inInternational journal of molecular sciences · 2021Article
- Scaffolding protein CcmM directs multiprotein phase separation in β-carboxysome biogenesis.Nature structural & molecular biology · 2021Article
- The state of oligomerization of Rubisco controls the rate of synthesis of the Rubisco large subunit in Chlamydomonas reinhardtii.The Plant cell · 2021Article
- Molecular basis for the assembly of RuBisCO assisted by the chaperone Raf1.Nature plants · 2020Article
- Duplication history and molecular evolution of the rbcS multigene family in angiosperms.Journal of experimental botany · 2019Article
- Article
- Article
- Roles of RbcX in Carboxysome Biosynthesis in the CyanobacteriumPlant physiology · 2019Article
- Rubisco Assembly in the Chloroplast.Frontiers in molecular biosciences · 2018Review
- From chaperonins to Rubisco assembly and metabolic repair.Protein science : a publication of the Protein Society · 2017Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The form I Rubisco of autotrophic bacteria, algae and plants is a complex of eight large (RbcL) and eight small (RbcS) subunits. It fixes atmospheric CO(2) in the dark reaction of photosynthesis. As shown for the cyanobacterial enzyme, folding of the RbcL subunits is mediated by the GroEL-GroES chaperonin system, and assembly requires the specialized chaperone RbcX, a homodimer of ~15-kDa subunits. Here we present the 3.2-Å crystal structure of a Rubisco assembly intermediate, consisting of the RbcL(8) core with eight RbcX(2) molecules bound. The structure reveals the molecular mechanism by which RbcX(2) mediates oligomeric assembly. Specifically, RbcX(2) provides positional information for proper formation of antiparallel RbcL dimers, thereby preventing RbcL-RbcL misalignment and off-pathway aggregation. The RbcL(8)(RbcX(2))(8) structure also suggests that RbcS functions by stabilizing the '60s loop' of RbcL in the catalytically active conformation.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.