ArticleThe Plant cell2021
Structural and biochemical analyses of concanavalin A circular permutation by jack bean asparaginyl endopeptidase.
Article in The Plant cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 26 citations in OpenAlex.
- Systematic discovery of circular permutations across the protein universe using CIRPIN.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Dual-Laser Laser-Induced Liquid Bead Ion Desorption Mass Spectrometry: A New Approach for Adjustable Softness and Higher Sensitivity.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026Article
- Concanavalin A targets phylogenetically conserved N-linked glycans on coronavirus spike proteins for broad-spectrum antiviral activity.Journal of virology · 2026Article
- Altering the carbohydrate-binding specificity of the legume lectin FRIL through structure-guided engineering.Nature communications · 2026Article
- Stimuli-Responsive Hydrogels: From Swelling-Deswelling Mechanisms to Biomedical Applications.Nanomaterials (Basel, Switzerland) · 2026Review
- A novel anti-CD20, concabody, enhances immunotherapy efficacy by targeting MPZL1 and augmenting antibody-induced cell death.Frontiers in oncology · 2026Article
- CIRPIN: Learning Circular Permutation-Invariant Representations to Uncover Putative Protein Homologs.bioRxiv : the preprint server for biology · 2025Article
- Article
- Computational insights into the circular permutation roles on ConA binding and structural stability.Current research in structural biology · 2024Article
- Structural Analysis and Characterization of an Antiproliferative Lectin fromInternational journal of molecular sciences · 2023Article
- Concanavalin A as a promising lectin-based anti-cancer agent: the molecular mechanisms and therapeutic potential.Cell communication and signaling : CCS · 2022Review
- Molecular insights into biogenesis of glycosylphosphatidylinositol anchor proteins.Nature communications · 2022Article
- Hololectin Interdomain Linker Determines Asparaginyl Endopeptidase-Mediated Maturation of Antifungal Hevein-Like Peptides in Oats.Frontiers in plant science · 2022Article
- Circular permutation of concanavalin A: why the rarest protein modification in nature came to be.The Plant cell · 2021Article
- Site-Specific Protein Modifications by an Engineered Asparaginyl Endopeptidase fromFrontiers in chemistry · 2021Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Over 30 years ago, an intriguing posttranslational modification was found responsible for creating concanavalin A (conA), a carbohydrate-binding protein from jack bean (Canavalia ensiformis) seeds and a common carbohydrate chromatography reagent. ConA biosynthesis involves what was then an unprecedented rearrangement in amino-acid sequence, whereby the N-terminal half of the gene-encoded conA precursor (pro-conA) is swapped to become the C-terminal half of conA. Asparaginyl endopeptidase (AEP) was shown to be involved, but its mechanism was not fully elucidated. To understand the structural basis and consequences of circular permutation, we generated recombinant jack bean pro-conA plus jack bean AEP (CeAEP1) and solved crystal structures for each to 2.1 and 2.7 Å, respectively. By reconstituting conA biosynthesis in vitro, we prove CeAEP1 alone can perform both cleavage and cleavage-coupled transpeptidation to form conA. CeAEP1 structural analysis reveals how it is capable of carrying out both reactions. Biophysical assays illustrated that pro-conA is less stable than conA. This observation was explained by fewer intermolecular interactions between subunits in the pro-conA crystal structure and consistent with a difference in the prevalence for tetramerization in solution. These findings elucidate the consequences of circular permutation in the only posttranslation example known to occur in nature.
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